ID W5W8S9_9PSEU Unreviewed; 425 AA.
AC W5W8S9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=KALB_3592 {ECO:0000313|EMBL:AHH96956.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH96956.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH96956.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH96956.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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}.
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DR EMBL; CP007155; AHH96956.1; -; Genomic_DNA.
DR AlphaFoldDB; W5W8S9; -.
DR STRING; 1449976.KALB_3592; -.
DR KEGG; kal:KALB_3592; -.
DR PATRIC; fig|1449976.3.peg.3616; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_11; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
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:UP000019225}.
FT DOMAIN 50..397
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46132 MW; 4E894E29EBC745CD CRC64;
MEYPQWGNGS VNGQAHSGTL LPDTTGPEVH LVGGSRAEAI KLAPVVDWMH RRARMRPVLV
DSGQHDSMFE QALGSFALRP DLRLRNDQGC TGQASHAEQL SGMVRLLDEH LMLRRPAAVV
AQGDTTTALA TALAAFWRGI PVVHLEAGLR SHNVRAPFPE ETTRRLVAQV STLHLAPTSR
AAENLRSEGL GGSGVLTVGS TAVDAAIRVS GRPVAFTDPR LEAVEWRARC GNCRLLVVTV
HRQESWGAPL AGVLNALTTL LQRHPDLEVV LPIHPHPALR KQVMTGLFGT DRVHVTAPLP
YDAFCRLLST ARLVLTDSGG VQEEAPIFGV PVLVLRENTE RVEAVEAGCS VLVGTEHRRL
ADHVSRLLQD SADRQAMVYA GNPFGDGHAG HRVEHAIAWM LGLEQTPPCP PQSVRYTPSE
RLRTE
//
