ID E9EXP6_METRA Unreviewed; 377 AA.
AC E9EXP6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|RuleBase:RU366046};
DE EC=5.1.3.2 {ECO:0000256|RuleBase:RU366046};
GN ORFNames=MAA_04795 {ECO:0000313|EMBL:EFY99866.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY99866.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY99866.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY99866.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose. {ECO:0000256|ARBA:ARBA00037676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00000083,
CC ECO:0000256|RuleBase:RU366046};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|RuleBase:RU366046};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU366046}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366046}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|RuleBase:RU366046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC family. {ECO:0000256|ARBA:ARBA00038238}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. {ECO:0000256|ARBA:ARBA00037955}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFY99866.1}.
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DR EMBL; ADNJ02000001; EFY99866.1; -; Genomic_DNA.
DR RefSeq; XP_007821082.1; XM_007822891.1.
DR AlphaFoldDB; E9EXP6; -.
DR GeneID; 19259081; -.
DR KEGG; maj:MAA_04795; -.
DR HOGENOM; CLU_007383_1_10_1; -.
DR OrthoDB; 5489993at2759; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR NCBIfam; TIGR01179; galE; 1.
DR PANTHER; PTHR43725; UDP-GLUCOSE 4-EPIMERASE; 1.
DR PANTHER; PTHR43725:SF51; UDP-GLUCOSE 4-EPIMERASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU366046};
KW Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW Isomerase {ECO:0000256|RuleBase:RU366046};
KW NAD {ECO:0000256|RuleBase:RU366046}.
FT DOMAIN 6..281
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 377 AA; 41684 MW; 18672617A62E138D CRC64;
MSAGTVLVTG GTGYIGSFTS LTLLENGYDV VIVDNLYNSS EVALDRIEKL CGRRPVFYKV
DITDEKALDH VFAKHPSIDS VIHFAALKAV GESGEIPLEY YRVNVGGSIA LLRSMERNNV
TNIVFSSSAT VYGDATRFPN MIPIPENCPT GPTNTYGRTK SMIEDVIRDC VNAQRNKLKK
ADQPFEQWNG ALLRYFNPCG AHPSGIMGED PQGVPYNLLP LLGQVATGKR EKLLVFGNDY
KSRDGTAIRD YIHVVDLARG HLAALKYLRE NKPGVKEWNL GSGRGSTVFE MIKAFSAVVF
GPENPEQLKY EIVARRQGDV LDLTANPALA NKELNWKTEL GMEKACEDLW RWVKNNPEGY
RQEPPAELLA AIKTPSS
//
