CAZyme Information: jhhlp_000332-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_000332-t41_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
887		98674.90	4.9953

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000002:603089-606405(-)

Full Sequence      

MKQWVSNQDGLDNLQLLDVAEPTELREGEVLVKINRVSLNYRDTEVVMGLYGHHKSLEEG
KKSIVPCSDICGTVVKVGPGNVEWREGDRVMATFNQGHLSGQVQEEHMGTGLGLPLQGCL
TQYRVFPDHGLVKVPNYLTDEEAAALPIAALTAWMSINTFQPFGQPQTGKDKVVLLQGTG
GVAISGLQIAHALGMTTIITSSSDAKLERAKTLGADYTINYKTYPDWDKKVMEITKGKGA
NVIFECGGAETLRKSFACVAFGGLISCIGYLSGKEDKSAGSMGINVLALSRNVTLKGILN
GPKDRFEEMLHFYNSKEIHPVIDREFEFEEAKEALKHLFSGSHFGKVIVKVAYFPNLHRH
LNPHKSNNMMKAIALFAVLLPAVLAQETETFTNPVVYEDFADNDVFLGPDGAYYFSASNM
HYSPGAPILRSYDLANWEFVGHSVPTLDFGERYNLTNGIAYRGGTWASTMRYRESTKLWY
WIGCVDFWYTYTYTASDPAGPWTRAAMSEGGRCYYDCGLFIDDDDTMYVVYGATDVRMAQ
LSPDGLSQVRTETIFSASDAGVDGIEGNRLYKKDGFYYILNDHPGSTTYIWRSESPWGPW
EYKILVDNIPSPVQWGGTPHQGSLIETPEGNWYYMSFTWAYPAGRMPVLAPVTWGCDGFP
TLVADENGGWGQTYPMPYPAQPLMNWTGTDTFQGSSLAPEWEWNHNPDETKYKVDNGLTL
STATVTDDFYKARNTLTHRIHGEFPVGTVHVDFSDMADGDIFGFAAFRDRSAAIEVFREG
DTYTLRARHNMTQEDSAWETVDQGTVVASEVLNTTEIWLQVSLDARPSGSKEATFHYSLD
GASFTALGGAYQLWTNWTYFMGYRYGIFNYATKALGGTIKVLSFTHA

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	392	660	8e-125	0.9962406015037594
CBM91	689	872	4.2e-16	0.88

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
176237	MDR7	3.68e-142	1	351	1	336	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.
350115	GH43_FsAxh1-like	5.65e-115	390	662	1	269	Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
223677	Qor	6.79e-72	4	351	5	326	NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only].
176227	Zn_ADH_like1	6.45e-62	9	351	10	342	Alcohol dehydrogenases of the MDR family. This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. 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.
176178	MDR	6.60e-60	29	313	1	271	Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family. The medium chain reductase/dehydrogenases (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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally 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. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC81418.1|CBM91|GH43_36	2.64e-228	389	880	51	545
AEO64951.1|GH43_36	2.55e-226	383	887	22	532
AEO64951.1|CBM91|GH43_36	2.55e-226	383	887	22	532
UPK98881.1|CBM91|GH43	1.43e-223	370	887	1	534
CEF78447.1|GH43_36	2.45e-221	382	887	22	532

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZXK_A	3.22e-138	384	884	1	529	Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXK_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
3ZXL_A	3.53e-137	384	884	1	529	Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXL_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
3ZXJ_A	1.39e-136	386	884	3	529	Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens],3ZXJ_B Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity [Humicola insolens]
6MLY_A	8.16e-61	392	877	22	501	Chain A, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_B Chain B, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_C Chain C, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_D Chain D, Bifunctional GH43-CE protein [Bacteroides eggerthii]
7VEM_A	8.42e-54	9	351	11	346	Chain A, the NADPH-assisted quinone oxidoreductase [Phytophthora capsici LT1534],7VEM_B Chain B, the NADPH-assisted quinone oxidoreductase [Phytophthora capsici LT1534]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94564|YGD6_SCHPO	2.38e-66	10	351	13	345	Zinc-type alcohol dehydrogenase-like protein C1773.06c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC1773.06c PE=3 SV=1
sp|T2KN85|PLH27_FORAG	1.27e-41	390	886	50	582	Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22160 PE=1 SV=1
sp|Q9WXE8|XYLO_PRERU	4.66e-33	390	866	40	482	Putative beta-xylosidase OS=Prevotella ruminicola OX=839 PE=3 SV=2
sp|O35017|YOGA_BACSU	1.57e-30	1	347	1	324	Uncharacterized zinc-type alcohol dehydrogenase-like protein YogA OS=Bacillus subtilis (strain 168) OX=224308 GN=yogA PE=3 SV=1
sp|E5AE42|YOGA_LEPMJ	4.24e-29	14	351	21	358	Zinc-type alcohol dehydrogenase-like protein YogA OS=Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) OX=985895 GN=Yog1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000000

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_000332-t41_1-p1.