ID N1MPA4_9SPHN Unreviewed; 369 AA.
AC N1MPA4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing) {ECO:0000256|ARBA:ARBA00038858};
DE EC=5.1.3.14 {ECO:0000256|ARBA:ARBA00038858};
GN ORFNames=EBBID32_30960 {ECO:0000313|EMBL:CCW18741.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW18741.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW18741.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW18741.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW18741.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW18741.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14;
CC Evidence={ECO:0000256|ARBA:ARBA00036080};
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000256|ARBA:ARBA00038209, ECO:0000256|RuleBase:RU003513}.
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:CCW18741.1}.
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DR EMBL; CAVK010000150; CCW18741.1; -; Genomic_DNA.
DR RefSeq; WP_006959927.1; NZ_CAVK010000150.1.
DR AlphaFoldDB; N1MPA4; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000013201; Unassembled WGS sequence.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR029767; WecB-like.
DR NCBIfam; TIGR00236; wecB; 1.
DR PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR PANTHER; PTHR43174:SF2; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003513};
KW Reference proteome {ECO:0000313|Proteomes:UP000013201}.
FT DOMAIN 22..367
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 369 AA; 39600 MW; CE4AA43BF29D65CE CRC64;
MKIAIVFGTR PEAIKMFPVI HALRARPGIE TRVIVTAQHR GLLDQVLEIA GIVPDVDLDV
MVPNQTLDGL TAKLIVELGK AFDAEKPDRI VVHGDTLTTM VASLAAYYRK IPVAHVEAGL
RSGDIHHPWP EEVNRRVVAC IADMNFAPTQ AAADALLRES RDAAGIHITG NTVIDALLAT
RDRVLADPSL ASGLDDLAAR FSGKRIIAVT SHRRENFGGG MEAIARSIAD IAARPDVAVI
FPVHPNPNVR PIMDAVLGDL PNVAMIEPLD YPHFVRLLDL CHLVLTDSGG VQEEAPSLGK
PVLVMRETTE RPEGVEAGTA KLVGADRTRI VREVLALLDD ADAYDAMARA HNPFGDGHAA
ERIAGVIAG
//