CAZyme Information: H257_13937-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_13937-t26_1-p1
• CAZy Family: GT8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2418		267366.04	6.8374

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913165:195777-203033(+)

Full Sequence      

MSFEGLSIAVTGGAGFIGSSLVTQLLALHATHVMIIDCLTPDYDVAIKRARIEYALTDER
CSFEQVNICDRARLLDVFRTHQPVVVYHLAAQAGVRRCELSPALTCATNVEGTASVLHTC
SATPSVKYVVFASSSSVYGNQPTPWNELTTPMDPQSLYARTKVMGEQLCQQFGAKHEGNK
SVCILRPFSVYGPQGRPDMAIAKFVRALRHRQPITLIGNTQRDCTFIDDVVQAFVLSALV
QRPHQERYKQQHQLVSATGESNINQTPLTRTFNVGTGHTTSMEDVLQQIQRAMRQVPVEV
LHAPANPVDAIVTRADSVAASNELGFRASVHLSEGIVKTVASELHDPPMHIAVVVATTDG
GRFDLLTKRCLPSIWNQTRPPDSIVIVADTSCEDGFTNDLHAFLRNSPGNVMLLFNHRTL
GASGAWNTGILHVLSAIPPGGDMSRMYIAICDDDDMWSCDHLALMDRHRSDVVVGGLIRY
ESDEGEGKPLSIPRLPLSSNAFLSGNPHLQGSNLYVRLLVLLQAGLFDEGLNACTDRDLM
VRVLDLPGVSVECVANGAHSVHHFADASRVRLTTCGHRKQLALTVFWRKHAHRMTKTVQG
DFMCRAVMLFGWSPPSPQVTPNESTTTSVPTPLISPSCDGRLSQKYALIVGITSDSGSSA
VRGLLEDLVALSCASLVSTDVVILENGPKASTLQATITTFQESHVLRCLFVPLDQQRQDM
VSGLLPPNQTFDVRASIAETRTRVQLYTSIFAHQLAPQLGSADCIVKPVVWILDDDKRLP
PTFPLQAVLQAHESDPTIAVVLGVDAQCPPLPPAFCVRTQLVDMLSHLQLCLHTPPSDPL
GPPQPPGATSLSEKVQGDYYHDLAGYKTLETPMWMNTMSTSLAHFTTLGECMNQILKGSL
VTRPLASDDDVPPTPTLTLTPSIHRGGCTFVFDLECMLDANTAPPCHRRSDMVWSLLQRD
VHHKRVVQCRQVCVNHIRQSMPSKTDLIDVAMKDVAGHALYQALQTVLGDPDMTETPSWV
ELWPRFWEQYCVTYNRRRTELRASVERIRGLVYTIKSLLRCQSAWWNSSNNSSDNDVIEG
AKATLWTALESLTHRFDSAWEEPLSVDVTNDNTMRELHMWFTAVLPRHRHDDWTRAQLTL
FHNSVYEPHRIESARACVSILYQVPPESLELLGVGYEGVTFHNGKSMDGQRGCCCFKYMD
LAALRFPNHVWDSLVALLTEPTKSMLGLRCVRRRGYHVCLERDYVDGTELNLNSKRECAP
EAPLSFLAWCRKANITCRNVKPQNLVVSRETGQLTLVDIGMDTVVPWTSEGEGHMMRKMY
LSWAWLHRHDLAALLSASHHSPKMPELQAGFNRFQLAYNHMLTPQACVDDAVALVAQLVP
PGGGSLLNVTIDWTLHARVQAILPHAQGAKLVVHPLVQVGKTELTLHNPFDTITCICVVC
AVDDLTMHRVLLELRAKVAPHGVVVLAMCNPFFVAANPSPHGLSDRFHRCFGRRNDDVVM
PRPWHVFEHAFWRAGLMVVDMAHTKSADVVAFEPVSDYIVVQLKPVTTLCLSPSVMPAAV
GGRPSHRGETTLMASCTLLIKTCATEHLTLAARVRHLKEQLEGPRAFAETLVIVDGYRRD
NDKSSFGKPEFFEPENELDEEYNDDLDSFVDSTPRPSLDTPLHRDTDKFDLCDGDAVTDE
LSKCLAVCQELQQEGWIDRYLHYQPTSAEVVALNSKWFGLHHNNQTHTRTRRGTLVQVAS
TLAGLEAATSEFILQVDSDLMVGRHSYYHLDDYLGQAMAIFAQDELAISVALDTFRSQPQ
GGGRQLPGGPTWCDPDTGTPHRVEVRGCVFSKARLMSKLPMPRPLGPTLAYLKSTTVTQY
HSVCKVDPQHWLLPWYRAMDIAMQDINWGRSYRVHDGTTFFVHPTDTTKASTDNYGLVLD
CVATLRLPSALQHGHVDCQGGVQDWMNALSKRHEDVVVVVLGRNVSPSKIMRCLDSIARQ
HKCPQWTVGVIVVDDASSSHTTAAFLRWYCHPQKNNARPPVTLIQPRFEPRKVGANTVLA
VEYVCANPMSVVVTLDMDDSLLGMDVWTTLYRYYIQEYADATVGGMLRTDKIQPPTSYPG
ICVNGARRLRGGGNVWMHLRSFRKYLFDRILDQDLREHAILDATTLTRGDNGGNPYLTFG
FDWAMMLPLVEMATKPTVVHEVLYLYEPFGPHKAETDAVAFRLLARPAYSKLRPLIAVVG
DANLNARHAVVDCAFPGPRASSEATGAAEKEAVLMALGQALVDAGYTVLCGGLGGAMLAV
ARGAHASTEWQEGRVVGLVPGTDRRQANSFIDMPIATGLGIARNCLVAQADAMVCVGGGS
GTLSEMALAWSAGRLVIGMESASGVTPQFVGKPLDGRRRYPAEVVPHDQVYRAKDVDQVI
QLLRAYLPLYAKKRQLPM

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187563	UDP_GE_SDE_e	3.27e-60	8	341	3	327	UDP glucuronic acid epimerase, extended (e) SDRs. This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.
187566	UDP_AE_SDR_e	3.71e-53	8	340	2	301	UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs. This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.
223528	WcaG	5.84e-52	8	345	3	310	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
396097	Epimerase	1.98e-48	8	248	1	235	NAD dependent epimerase/dehydratase family. This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
212494	SDR_e	1.31e-43	8	238	1	187	extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AKU11317.1|GT2	2.64e-170	322	2208	3	1722
AGB01185.1|GT2	8.31e-131	350	2196	3	1703
VEJ15080.1|GT2	3.83e-103	353	2412	6	1782
ACY13523.1|GT2	3.13e-75	347	1083	25	764
BBM87114.1|GT2	1.44e-67	351	1008	8	634

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U4Q_A	4.43e-32	10	336	8	324	Chain A, dTDP-glucose 4,6-dehydratase [Klebsiella pneumoniae],5U4Q_B Chain B, dTDP-glucose 4,6-dehydratase [Klebsiella pneumoniae]
6KV9_A	2.06e-24	8	336	21	315	MoeE5 in complex with UDP-glucuronic acid and NAD [Streptomyces viridosporus ATCC 14672],6KVC_A MoeE5 in complex with UDP-glucose and NAD [Streptomyces viridosporus ATCC 14672]
6LTT_A	2.31e-24	10	350	5	315	Chain A, UDP-glucose 4-epimerase [Mycobacterium tuberculosis H37Rv],6LTT_B Chain B, UDP-glucose 4-epimerase [Mycobacterium tuberculosis H37Rv]
6ZL6_A	2.16e-23	6	336	1	303	Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP and NAD [Bacillus cereus HuA2-4],6ZL6_B Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP and NAD [Bacillus cereus HuA2-4],6ZLA_A Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD [Bacillus cereus],6ZLA_B Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD [Bacillus cereus],6ZLA_C Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD [Bacillus cereus],6ZLA_D Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD [Bacillus cereus],6ZLD_A Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid and NAD [Bacillus cereus HuA2-4],6ZLD_B Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid and NAD [Bacillus cereus HuA2-4],6ZLK_A Equilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid/UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLK_B Equilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid/UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLK_C Equilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid/UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLK_D Equilibrium Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Glucuronic acid/UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLL_A Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLL_B Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLL_C Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4],6ZLL_D Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with UDP-Galacturonic acid and NAD [Bacillus cereus HuA2-4]
6ZLJ_A	7.17e-23	6	336	1	303	Crystal Structure of UDP-Glucuronic acid 4-epimerase Y149F mutant from Bacillus cereus in complex with UDP-4-DEOXY-4-FLUORO-Glucuronic acid and NAD [Bacillus cereus],6ZLJ_B Crystal Structure of UDP-Glucuronic acid 4-epimerase Y149F mutant from Bacillus cereus in complex with UDP-4-DEOXY-4-FLUORO-Glucuronic acid and NAD [Bacillus cereus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P39858|CAPI_STAAU	1.58e-31	6	243	1	234	Protein CapI OS=Staphylococcus aureus OX=1280 GN=capI PE=3 SV=1
sp|O81312|GAE3_ARATH	1.50e-29	4	338	89	413	UDP-glucuronate 4-epimerase 3 OS=Arabidopsis thaliana OX=3702 GN=GAE3 PE=2 SV=1
sp|O22141|GAE4_ARATH	3.05e-29	4	340	95	421	UDP-glucuronate 4-epimerase 4 OS=Arabidopsis thaliana OX=3702 GN=GAE4 PE=1 SV=1
sp|Q04871|YCL2_ECO11	3.67e-29	10	336	5	321	Uncharacterized 37.6 kDa protein in cld 5'region OS=Escherichia coli O111:H- OX=168927 PE=3 SV=1
sp|Q9LPC1|GAE2_ARATH	7.07e-29	4	340	90	416	UDP-glucuronate 4-epimerase 2 OS=Arabidopsis thaliana OX=3702 GN=GAE2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000028	0.000002

TMHMM  Annotations     

There is no transmembrane helices in H257_13937-t26_1-p1.