CAZyme Information: RhiirA1_442609-t46_1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: RhiirA1_442609-t46_1-p1
• CAZy Family: PL38
• CAZyme Description: NAD(P)-binding protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1074	LLXH01000595|CGC1	124282.93	6.4371

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisA1DAOM664342	26582	N/A	106	26476

• Gene Location: location=LLXH01000595:15175-19639(+)

Full Sequence      

MVSEKRVILITGGNGFIGSHVAKRLHDQGYYVRVIDLHDDPTFRLYKDTSEFCSEFIEGD
IRSIETCRKLFNKNDVKWVFHFAANMGGVGVINSKNNFVIYQENHIMSLNILQVSMQSNI
EKFFYASSACVYPYNKQINLNEDIKLKEDDSTWNCNSIDTKPQESYGAEKLNTEIFISSL
RELSTSSENKTTSKFPQFKIARFHNVYGEGGTWYGGREKAPAALLRKAICASKYTKENVI
EIWGNGKQRRSFLYIADCVDAIIKFMKSDLDLTLNIGSEESIRIDELACVAFETVGVTRD
KVTLKFDESKPIGVNNRNSDNTLVSKYLDWYPKHTIREGMEKTSLWIQQELEKQRHQYKD
DSWNELVRTYLESKVDVLNYNNETITFGVLLPITSRGLTKPEDCLENLSNFAKSLYETSQ
EDIQDRFGETRYQIKIYVGIDNDDSLFHPIKNNPAERILNEHGFTDIHTMEFDFPPGSIC
EIWIELARKAYDDNCDYFILFGDDVIIETNGWMNKFHEAYRKISIQKKVPRGFGCITFTD
TSFHGFPTFPVIGRVHLDIFNGEVLPRKTFKNQDGDPYLFQTYRRWGCSMMLEDVEIQNV
VGGSLDPRYERTHHPNWSFDILNNSVNRVEEWLKKNCKNPIPKLLTLDVIVPSYRVNLKY
LDPMISLKKPVTMSTTTIIIVDDPNSSNIITLKKFYEKDPFIRIRVNKTNLGASLSRNRG
LRESNADYVLFFDDDVVPEKNILFECEKIIKKHPNACGFIGNTKFPPADGSIYTSALALS
GLTFFWGISELWDDDVPWGVTANLLIRRFNENILYDPVFPKTGGGEDIDFCLKQRNFFIK
NTKNGKGFQAAPNVMATHPWWNNGNRDYWRFYKWATGDGALVKMYPELTYNDIVPNSIEL
LFGTILFFLVSMIFSLFFAVFYNTPIINTFTILTFLSIPLVIVSSIIADMYLHLTEQPYK
HTSTVGGYRYILAMVESSLIRIMSEFGRLMGMIERNEWGYIGKRFDWFVKRKEGSVWTER
YNNLRKFLIWFVVTESLTEAYMSQPFKKLDIVIIIINMTFFSVLNDYEAQDLLS

Enzyme Prediction     

No EC number prediction in RhiirA1_442609-t46_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
178298	PLN02695	7.97e-92	3	354	19	336	GDP-D-mannose-3',5'-epimerase
187581	GME-like_SDR_e	1.70e-87	8	355	3	320	Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs. This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. 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	1.90e-47	8	353	3	314	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
187566	UDP_AE_SDR_e	3.28e-40	8	347	2	304	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.
396097	Epimerase	2.89e-38	8	277	1	238	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV90438.1|GT2	5.88e-279	7	1033	18	1011
QRV75675.1|GT2	4.77e-275	6	1029	17	1007
QRW04585.1|GT2	3.57e-261	6	1029	18	1011
QRW23776.1|GT2|GT8	5.94e-223	7	989	13	924
UFH56504.1|GT2	6.66e-35	646	901	25	272

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C59_A	4.58e-67	3	362	27	353	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), with gdp-alpha-d-mannose and gdp-beta-l-galactose bound in the active site. [Arabidopsis thaliana],2C59_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), with gdp-alpha-d-mannose and gdp-beta-l-galactose bound in the active site. [Arabidopsis thaliana]
2C54_A	1.18e-66	3	362	27	353	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana),k178r, with gdp-beta-l-gulose and gdp-4-keto-beta-l-gulose bound in active site. [Arabidopsis thaliana],2C54_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana),k178r, with gdp-beta-l-gulose and gdp-4-keto-beta-l-gulose bound in active site. [Arabidopsis thaliana]
2C5A_A	1.62e-66	3	362	27	353	GDP-mannose-3', 5' -epimerase (Arabidopsis thaliana),Y174F, with GDP-beta-L-galactose bound in the active site [Arabidopsis thaliana],2C5A_B GDP-mannose-3', 5' -epimerase (Arabidopsis thaliana),Y174F, with GDP-beta-L-galactose bound in the active site [Arabidopsis thaliana]
2C5E_A	3.04e-66	3	362	27	353	gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), k217a, with gdp-alpha-d-mannose bound in the active site. [Arabidopsis thaliana],2C5E_B gdp-mannose-3', 5' -epimerase (arabidopsis thaliana), k217a, with gdp-alpha-d-mannose bound in the active site. [Arabidopsis thaliana]
4ZRM_A	6.30e-21	8	352	6	312	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|A2Z7B3|GME1_ORYSI	1.44e-68	3	360	27	350	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. indica OX=39946 GN=OsI_032456 PE=2 SV=1
sp|A3C4S4|GME1_ORYSJ	1.98e-68	3	360	27	350	GDP-mannose 3,5-epimerase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=GME-1 PE=1 SV=1
sp|Q93VR3|GME_ARATH	2.23e-66	3	362	25	351	GDP-mannose 3,5-epimerase OS=Arabidopsis thaliana OX=3702 GN=At5g28840 PE=1 SV=1
sp|Q2R1V8|GME2_ORYSJ	4.84e-66	4	355	21	338	GDP-mannose 3,5-epimerase 2 OS=Oryza sativa subsp. japonica OX=39947 GN=GME-2 PE=2 SV=2
sp|G4WJD3|COLC_YERPU	8.22e-22	8	343	3	297	GDP-L-colitose synthase OS=Yersinia pseudotuberculosis OX=633 GN=colC PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000076	0.000000

TMHMM  Annotations     

Start	End
900	922
929	951