CAZyme Information: PIW_T001129-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T001129-RA-p1
• CAZy Family: AA17
• CAZyme Description: Alcohol dehydrogenase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
987		108333.80	6.7409

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC00079:10292-14867(-)

Full Sequence      

MCARKAGQRSRCARAFSLLRWCGTSWRQCMHSLRVARSLLSVLSPQLQALVEASLGDSLA
RSSTTTLSQSSAGASAALHTATAAESDNPSPTAEKRAATTTTLSTELRDGAQHDRVPVSF
KLNPSELFVLRHPASPGFVVKQNFLGSTGATAVRDALLALAETETFQEAKVGHGDHLRSA
RAVRGDRIHWLKRPGDLSQSAGSDGPHPAILHLMESVESLVYGVKSAVPSLNIRNVTSTQ
LAIFPGGGARFVRHADAYSSAHHEDASRSSPSSLDGLVRVLTCVYYLNDHWEPNHGGQLR
VYVDGSSSSSSSSSSSLVAAAAGVAHWDVAPALDTLVVFRGLDVEHEVLPAFRERMALTI
WYYGRVESQPATHPSRIRIGICLQDDNDDDTRQYLEDKYSADQIDSHMRFRAGWDAFLIN
QLEKCPSAKPILTTYPLGYTLPNNVSTDIRPTLLCASSFDEHGILRQASKTLTRVSPVPL
ASSFWAAGFAFSSARVISEVPYDESLRFLFFGEEASMNARLWTAGWDFFTPGESVVYHLW
TRSYRRVFQEIEDQETVKWRAASQQYVKTLLTHSSNADSEASGSEQPELSAGKYSLGVER
SLSTYQSRIGVSFEKQKIRWEAEWGNLDPIHFELSARAADMTETPPAVIPPTFRAYQYEQ
CGDPFEEIKLRTGIRQTSLQPHDVRIQVISAALNPVDYKLVEGSRHAQLGRKPSHETPFT
VGFDLAGVVVEVGLSVADLKVGDHVFAMMPWLKFGSFAEYAVVNEEYVAHKPEALSFDEA
AGVPLAATTSFQVLFQHAKLQPGERVLILGGSSATGIFGIQLAKAAGAYVIATTSFRNTT
FVEGLDADQVIDYTQESWGDVLAQHSVDVIYDCGMEPDAWSRVAQQVLKKHTGRFVSLLP
SPSNNSRQIESRSGATNLGQIMVNPTAAHLREIAKLFDNKSLVAPVDSVYEFDELFDAIR
KLKTGRARGKLILHVHSPPPHHYPADH

Enzyme Prediction     

EC	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT60	403	614	1.6e-62	0.6515151515151515

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176191	MDR_like_2	7.25e-99	654	973	2	309	alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases. Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
176228	MDR1	3.38e-96	681	973	26	319	Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
176210	RTN4I1	9.14e-66	654	972	2	348	Human Reticulon 4 Interacting Protein 1. Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.
176211	enoyl_reductase_like	9.97e-66	678	975	23	339	enoyl_reductase_like. Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
223677	Qor	5.35e-65	653	975	1	326	NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA15104.1|GT60	1.14e-110	122	637	89	641
UIZ23002.1|GT60	8.54e-55	479	634	15	163
BDA44136.1|GT60	3.34e-52	174	625	97	595
CAG4710602.1|GT60	1.61e-41	127	634	60	661
AAK56291.1|GT60|2.4.1.-	1.25e-36	403	558	100	267

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4IDA_A	8.34e-39	645	974	16	330	Structure of the Fragaria x ananassa enone oxidoreductase in its apo form [Fragaria vesca],4IDB_A Structure of the Fragaria x ananassa enone oxidoreductase in complex with NADP+ [Fragaria vesca],4IDC_A Structure of the Fragaria x ananassa enone oxidoreductase in complex with NADPH and HDMF [Fragaria vesca],4IDD_A Structure of the Fragaria x ananassa enone oxidoreductase in complex with NADPH and EHMF [Fragaria vesca],4IDE_A Structure of the Fragaria x ananassa enone oxidoreductase in complex with NADP+ and EDHMF [Fragaria vesca],4IDF_A Structure of the Fragaria x ananassa enone oxidoreductase in complex with NADPH and HMF [Fragaria vesca]
2VN8_A	2.60e-34	681	975	50	374	Crystal structure of human Reticulon 4 interacting protein 1 in complex with NADPH [Homo sapiens],2VN8_B Crystal structure of human Reticulon 4 interacting protein 1 in complex with NADPH [Homo sapiens]
3TQH_A	5.48e-31	654	975	8	320	Structure of the quinone oxidoreductase from Coxiella burnetii [Coxiella burnetii]
5A3J_A	3.32e-29	682	973	34	327	Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_B Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_C Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_D Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_E Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_F Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_G Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_H Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_I Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_J Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_K Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3J_L Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13-Oxo-9(Z),11(E),15(Z)- octadecatrienoic acid. [Arabidopsis thaliana],5A3V_A Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana [Arabidopsis thaliana],5A3V_B Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana [Arabidopsis thaliana],5A4D_A Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_B Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_C Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_D Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_E Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_F Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_G Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana],5A4D_H Crystal structure of the chloroplastic gamma-ketol reductase from Arabidopsis thaliana bound to 13KOTE and NADP [Arabidopsis thaliana]
3GAZ_A	4.44e-26	651	975	6	335	Crystal structure of an alcohol dehydrogenase superfamily protein from Novosphingobium aromaticivorans [Novosphingobium aromaticivorans DSM 12444],3GAZ_B Crystal structure of an alcohol dehydrogenase superfamily protein from Novosphingobium aromaticivorans [Novosphingobium aromaticivorans DSM 12444]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q84V25|ENOXE_FRAAN	1.35e-38	641	974	1	319	2-methylene-furan-3-one reductase OS=Fragaria ananassa OX=3747 GN=EO PE=1 SV=1
sp|K4BW79|ENOX_SOLLC	1.80e-38	629	974	56	385	2-methylene-furan-3-one reductase OS=Solanum lycopersicum OX=4081 GN=EO PE=1 SV=1
sp|Q8T1C6|GNT1_DICDI	1.65e-37	403	558	100	267	[Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase OS=Dictyostelium discoideum OX=44689 GN=gnt1 PE=1 SV=2
sp|Q7T3C7|RT4I1_DANRE	4.91e-37	681	975	57	381	Reticulon-4-interacting protein 1 homolog, mitochondrial OS=Danio rerio OX=7955 GN=rtn4ip1 PE=2 SV=2
sp|Q941I0|ENOXC_FRAAN	9.93e-37	641	974	1	320	2-methylene-furan-3-one reductase OS=Fragaria ananassa OX=3747 GN=EO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PIW_T001129-RA-p1.