CAZyme Information: P175DRAFT_0506434-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0506434-t39_1-p1
• CAZy Family: GH53
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
779		86465.04	5.2294

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000001:3603840-3607163(-)

Full Sequence      

MGTPLVGTAIITGGNGSLGSEIAVAIAKTQPFVHLLLLARDIRSESVQNVRERIRLIGPR
SIEVARVDLASFNSVASFAENTVERVHSKDIPPVTLLINCAAMSSYVTDQVTRDGHDPVY
QTNCIAPFLLTVSLLEAFRAGDGTPNGGARVINIGCSSISKGSLGYFEDEDQASHVGRSG
TPLSAKDALARVGSSKLIMSAAMYALRRSLVLTGNISLNIYTLDPGGMVGESHLVADVPL
SIRMAHQTKSGLRPFLRVFSKSAINKVSVPAKVIAKVAFQSDTVENWGRERYYILDSEYE
AGSVIPALRDPPQMEALLNKLMRQVELFQRLCFIAGVSLFVLLLIFPSWRASILPVLSLG
LLSSSPEDLHIQTVRYYDLVKMQGTASGWENGERVLMCTPLRDAASHLPMFFSHLRNLTY
PHHLIDLAFLVSDSKDGTMEMLSQMLEELQHDPDRDMSFGEISVIQKDFGQKVNQDVESR
HGFAAQAGRRKLMAQARNWLLSATLRPTHSWVYWRDADVLTAPSTIIEDLMRHDRDVIVP
NVWRPLPDWLGGEQPYDLNSWQESETALALADTLDEDAVIVEGYAEYATWRPHLAYLRDP
YGDPDMEMELDGVGGVSILAKAKVFRSGVHFPAFSFEKHAETEAFGKMARRMGFSVIGLP
HYTIWHLYEPSVDDLRHMEEMEQERKQREEEERVQSERAERNKAMFQDPKIESEIDNAFV
RDSMEEAAREQPARQVSTPQDPEDSSAAAGEPATAKGKADDVHEQQGNLAKTDEAAKSS

Enzyme Prediction     

No EC number prediction in P175DRAFT_0506434-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT62	372	635	2e-125	0.9888059701492538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397491	Anp1	8.75e-161	373	635	1	265	Anp1. The members of this family (Anp1, Van1 and Mnn9) are membrane proteins required for proper Golgi function. These proteins co-localize within the cis Golgi, and that they are physically associated in two distinct complexes.
212492	retinol-DH_like_SDR_c_like	5.29e-27	8	261	3	220	retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
187585	carb_red_PTCR-like_SDR_c	4.08e-12	8	226	2	178	Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs. PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
212491	SDR_c	1.03e-11	9	160	1	135	classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
235737	PRK06197	2.69e-11	8	154	18	150	short chain dehydrogenase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA64203.1|GT62	0.0	1	770	1	777
BCS20027.1|GT62	1.20e-235	323	726	39	441
BAE60428.1|GT62	7.73e-233	321	737	12	427
QRD89585.1|GT62	7.87e-233	321	737	37	452
UDD59518.1|GT62	1.92e-232	321	737	37	452

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZF8_A	8.58e-60	374	671	6	304	Crystal structure of Saccharomyces cerevisiae Mnn9 in complex with GDP and Mn. [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P32629|ANP1_YEAST	5.35e-156	366	686	54	374	Mannan polymerase II complex ANP1 subunit OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ANP1 PE=1 SV=3
sp|O74745|ANP1_SCHPO	7.09e-151	374	687	77	392	Mannan polymerase II complex anp1 subunit OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=anp1 PE=3 SV=1
sp|P23642|VAN1_YEAST	4.60e-122	373	686	171	531	Mannan polymerase I complex VAN1 subunit OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=VAN1 PE=1 SV=3
sp|Q00314|VAN1_CANAX	1.40e-118	367	686	69	438	Vanadate resistance protein OS=Candida albicans OX=5476 GN=VAN1 PE=3 SV=1
sp|P53697|MNN9_CANAL	2.82e-62	367	669	66	368	Mannan polymerase complex subunit MNN9 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN9 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000000

TMHMM  Annotations     

Start	End
331	353