CAZyme Information: I303_06171-t42_1-p1

Basic Information

• Species: Kwoniella dejecticola
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella dejecticola
• CAZyme ID: I303_06171-t42_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1143	KI894033|CGC9	127750.24	5.8350

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KdejecticolaCBS10117	8724	1296121	122	8602

• Gene Location: location=KI894033:1402421-1406222(-)

Full Sequence      

MPPPLGKVISAIFHKPRYLALLILIPLAALLYRQWSDFDSHSPRPIKVTGGTTHSPWEGL
AELAEDEDELGTWYPGGVGDWLSWKQDTRKTLLITAGAGQIGQSLIPSLIDDYIVHVIDI
APRPATFPASVIYHKDSILSSSPALSDLFASSSFDGVIHLAAVSLEAWCAPKENECHEVN
VEGTKHLLDQIGTTLSKSRKRICSRGVKTPWIIMGSSMDVYPQEQGVSELSGKNPANALG
RTKLDAETALQDFISSTSTEGIVHGMILRFPEVYGYPQHRSIPHAFIPSLLTNALTSLPI
QYSSDIPSLDLLHIDDAIKGIRKAISRIGDPAKFGAEKDGEVEEFNLVYGKRWQTQDIVE
LLRTEAHSMSPLRDIGSASSPQMPNFSNERAKEKLGWEPELSAPVGLGLALQTLSEDIAE
YSRTWHQNHCSPTADFPAENGHLIDHFVEDERNKELTKLDGCTVNLGFDHDGWIHHVKCE
DGRHCTADGEKVTAMNWNQSVFIVHKVSGANKNERTARVIFEEEKGMGYLGYRRDDQDEV
GLELFPKTSLEGQMEFDVEVNRHGSFLRLLIPNTGKQIHALSNSTDSSTYFTLEPTTKWI
DPHFDTRMNILCCPSEGDWPLLLDDYESADIRFGSTGQIPFNSSRRLHLCGQAEKAVMHN
FDRLSVAKQAVNKVENGQEAHVWKGDHGANTKSQPHSWALKDLPACYNDCNSPAICIQTG
ECKCVQADHCQPKRENPILSLYPIASPDSDTGKGKSHLGSLAGYSPILVNAVNKTDWRDI
LLPAAREALRVNPNFIKVHVADGYKGQETIEASSCHNLQTKHCFSADSIMYKALRHLQVP
AEEAELIIVPVYQQCKGTEFLLHDGMHHALESIPGSKTGEKTIALVLTHDWGICVAFAWE
IWSAREQPLYPDWILNNVLVWSVMGDYDSPCYRPHQDVVIPARTCQSINLKDHFSDIRQV
KPARERDHLLTWSGTYWGTGKSDRLRLTCDRGGAGERELVKGKGPQSSFENWDYMNDLNN
ARFCPQPRGIAGWSPRTNDAIYAGCIPVLIAEGSHYPFVNYLDWSKFSVRIAPTELDRLE
QILAAIPLWKVEEMQANLVAVREAFIYSTDEHPEDELDRRGPMFFALHEAAFKVRTRYPV
EED

Enzyme Prediction     

No EC number prediction in I303_06171-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT47	796	1086	1.6e-39	0.9831081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397245	Exostosin	7.58e-54	793	1086	2	290	Exostosin family. The EXT family is a family of tumor suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.
223528	WcaG	2.47e-33	90	412	1	306	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
396097	Epimerase	5.18e-22	93	331	2	231	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	5.40e-22	93	347	2	199	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.
187551	UDP_G4E_3_SDR_e	1.16e-16	93	403	2	295	UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs. Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. 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
ADV23625.1|GT47	0.0	15	1143	17	1129
KGB76296.2|GT47	0.0	15	1141	17	1127
AAW44475.1|GT47	0.0	3	1143	6	1131
UOH83106.1|GT47	0.0	3	1143	6	1124
AFR96705.1|GT47	0.0	3	1143	6	1124

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C20_A	6.23e-11	90	427	2	322	Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis],2C20_B Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis],2C20_C Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis],2C20_D Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis],2C20_E Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis],2C20_F Crystal Structure Of Udp-Glucose 4-Epimerase [Bacillus anthracis]
4ZRM_A	2.30e-09	88	412	2	305	Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) from Hyperthermophilic Eubacterium Thermotoga maritima [Thermotoga maritima MSB8],4ZRM_B Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) from Hyperthermophilic Eubacterium Thermotoga maritima [Thermotoga maritima MSB8],4ZRN_A Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) with UDP-glucose from Hyperthermophilic Eubacterium Thermotoga Maritima [Thermotoga maritima MSB8],4ZRN_B Crystal Structure of UDP-Glucose 4-Epimerase (TM0509) with UDP-glucose from Hyperthermophilic Eubacterium Thermotoga Maritima [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8S1X9|GT13_ORYSJ	8.69e-20	821	1115	80	381	Probable glucuronosyltransferase Os01g0926400 OS=Oryza sativa subsp. japonica OX=39947 GN=Os01g0926400 PE=2 SV=1
sp|Q9ZUV3|IRX7_ARATH	2.65e-18	820	1115	116	424	Probable glucuronoxylan glucuronosyltransferase IRX7 OS=Arabidopsis thaliana OX=3702 GN=IRX7 PE=2 SV=1
sp|Q8S1X8|GT14_ORYSJ	4.76e-17	822	1115	74	374	Probable glucuronosyltransferase Os01g0926600 OS=Oryza sativa subsp. japonica OX=39947 GN=Os01g0926600 PE=2 SV=1
sp|Q7XLG3|GT42_ORYSJ	2.08e-15	822	1115	79	379	Probable glucuronosyltransferase Os04g0398600 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0398600 PE=2 SV=2
sp|Q6H4N0|GT21_ORYSJ	2.30e-15	784	1115	54	392	Probable glucuronosyltransferase Os02g0520750 OS=Oryza sativa subsp. japonica OX=39947 GN=Os02g0520750 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999702	0.000325

TMHMM  Annotations     

There is no transmembrane helices in I303_06171-t42_1-p1.