CAZyme Information: FOMG_07718-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_07718-t38_1-p1
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1245	JH659333.1|CGC13	138810.61	5.4173

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659333.1:202245-207274(+)

Full Sequence      

MAYFQNFLTTLLLFQCYQSFPGALAGFEETLVAFEPSIGATEIQDAVILRDDSDPFGIAI
AVGSLADDFEQITGTRPSVRAWAGDNSTTSEVKVASESAIIAATVDSPLMRQLESSRKLN
LSSIRGKWETFETTLVAQPLPGVQNALVIAGSDMRAVIFGIFTLSEQSGQSPLYWWNDVP
AKKHDKIYAINKTLTFGEPTVKYRGIFINDEAPALTSWWAQRSRREDYTFDSEFYERVFD
LLLRLRANLIWPAMWGSFVPAPGRIFFTDDPGNMALANDYGIVVSTSHHEPMQRASNEWK
QSKNGAWDWVANKGNVVEFMREGVRRAGGNDTYFTLGMRGENDGPIQADDPIAVLREVFA
VQRNILASFYGNETAARQIWTIYKEVATYYAAGLEPPEDVTLMFTDDNWGNVQKLPNAKE
LDRSGGIGMYYHFEYVGRPKSWKWQNCNNLPKIYKELFQAAQAGANRIWVFNVGDIKPVE
LPLNMAMDLAWNATRFDLDSLPDYLQSLAARDFDLEHSEVIASGWLAYSHLVGMRKFEML
EPTTYSITNYEEADRILGAWKALADRVRAIEASLPQTHRDAFFHSSTYAAVAGYNYHAIL
IGQGKNRQYSFERRNSANAIAYDLIERFEYDHDLTIEYDAIAGGKWRGIMSTPKFDMSTA
DWRPSSRDVMANLSFVQLRQDFDYAFGNLGIYVEQSRAPYLQGRICASINPSKPTKDGLS
PMMRPMEPHGPAFRWIDLFHRGDHRRPIRWSISVPEPWINVSQVSGEVSGSKPEERVHIS
INWELVPATYNQTVQLRVFYGPPAHFDDVHLPVINIRAPKDFAGFPEVDGIISIEAPHYQ
RSSLTQDTGRNIGFKVMPRLASRSESGSVALRPYQAAIESESESKASWLEYDIFILGNAT
RPAINATIYINGALDTRADKPMLCSLSLQNESKPANDFFKILGTPEKAGDTPPEWNAEVA
NGVWTRTLQLGSLSPGFGLEIARRALTKGHRVIATSRNPKKNEGHVQEIESKGGRWIALD
VTAPDLSSVVDKAKALYGTIDILVNNAGFSLNGGFEDLSEDDLRAQFETNVFGVFKMMKA
VLPGMRERQSGIVINIGSTGGLRSLPGVSLYASSKHALEGLTEAVWHEYRDFNVKIVLVE
PGPFRTNFLGENAAVIRPISSFYKGTSTETTLNHLKDSHVDQPGDPIKAATIIVDYALGE
GSAKGSNEFLRLPLGSGALKTVQGKIESLEENLAGVREMAQSTDF

Enzyme Prediction     

EC	3.2.1.131:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	44	674	1.5e-209	0.836441893830703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
406396	Glyco_hydro_115	0.0	197	539	1	334	Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
187632	17beta-HSD-like_SDR_c	7.32e-72	974	1219	9	248	17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 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.
180446	PRK06180	2.18e-69	974	1245	13	277	short chain dehydrogenase; Provisional
395056	adh_short	5.66e-51	976	1151	11	189	short chain dehydrogenase. This family contains a wide variety of dehydrogenases.
180744	PRK06914	6.35e-51	974	1218	12	255	SDR family oxidoreductase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD58010.1|GH115	0.0	1	1245	1	1278
UQC81939.1|GH115	0.0	28	976	24	981
BAE63119.1|GH115	0.0	23	976	16	934
UDD61142.1|GH115	0.0	23	749	16	742
VBB79496.1|GH115	1.62e-302	22	976	16	980

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZMH_A	2.81e-153	40	836	17	772	Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
7PUG_A	5.64e-133	48	654	28	629	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A	4.07e-131	48	654	27	628	Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4C90_A	6.25e-126	48	650	55	640	Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
6NPS_A	5.76e-104	46	980	20	942	Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0CU71|CLAN_PASFU	7.14e-37	974	1172	11	207	Oxidoreductase claN OS=Passalora fulva OX=5499 GN=claN PE=2 SV=1
sp|P37959|YUSZ_BACSU	3.79e-32	974	1222	12	259	Uncharacterized oxidoreductase YusZ OS=Bacillus subtilis (strain 168) OX=224308 GN=yusZ PE=3 SV=2
sp|A6SSW9|BOA17_BOTFB	2.78e-31	974	1200	11	235	Oxidoreductase BOA17 OS=Botryotinia fuckeliana (strain B05.10) OX=332648 GN=BOA17 PE=2 SV=1
sp|Q9NYR8|RDH8_HUMAN	1.57e-28	966	1180	6	221	Retinol dehydrogenase 8 OS=Homo sapiens OX=9606 GN=RDH8 PE=1 SV=1
sp|P0CU82|CALM_PENDC	3.18e-26	974	1240	23	293	Oxidoreductase calM OS=Penicillium decumbens OX=69771 GN=calM PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.517531	0.482453

TMHMM  Annotations     

There is no transmembrane helices in FOMG_07718-t38_1-p1.