ID Q48A39_COLP3 Unreviewed; 760 AA.
AC Q48A39;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=UDP-N-acetylglucosamine 2-epimerase/UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000313|EMBL:AAZ25607.1};
GN OrderedLocusNames=CPS_0308 {ECO:0000313|EMBL:AAZ25607.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ25607.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ25607.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ25607.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000256|RuleBase:RU003513}.
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DR EMBL; CP000083; AAZ25607.1; -; Genomic_DNA.
DR RefSeq; WP_011041181.1; NC_003910.7.
DR AlphaFoldDB; Q48A39; -.
DR STRING; 167879.CPS_0308; -.
DR KEGG; cps:CPS_0308; -.
DR eggNOG; COG0381; Bacteria.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_017307_0_0_6; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR InterPro; IPR029767; WecB-like.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR NCBIfam; TIGR00236; wecB; 1.
DR PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR PANTHER; PTHR43174:SF1; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU003513};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 677..758
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 760 AA; 82946 MW; E355D2ACF2618648 CRC64;
MKIGIIVGTR PEIIKMAPVI RECKKRGIAY FIIHSNQHYS QEMDSIFFKE LELPAPDYNL
GVGSGLHSNQ TGNILIEMEP ILLQEKPDVV LVQGDTNTVL AGALAASKLD IKVGHIEAGL
RSYDRTMPEE TNRILTDHMS EYLFAVGPNQ HAILAKEGID SDKIFTVGNT VSDSLFQHLD
ISASTSTILA DLDVTSGEFF LVTAHRASNV DIPANLLELL ALFDKLHAKY SQTIVWPIHP
RTQSKLKEFS IELPSYLKLI PPIGYLDFIQ LQKHAQLILT DSGGIQEEAC LLGVPCITLR
ENTERPESIE VGANVLVGRD AVKALAAADK WLASDAASFS WSNPFGDGHV AETILDIITN
SVPNTLEEEI IAKNETLSVI GMGYMGLPIA SLLAEAGYKV TGVDLNSDKV SVINEAQCPF
DEAGLPELIT KVVSQGFLTA STEIPSSETY LVAVPTPHKN NSCDRSYVFS AVDAIAKVAK
NGQTVIVEST ISPQTSVAVA QRFADAGLTI DVVHCPERAI PGQTLHELVH NDRIIGATSI
EAQQKVKTIY QSFVKGEVFL TDLTTAECIK LVENTSRDVG IAFANELSQI CEELEVDVYE
VIRLANRHPR VNVLTPGPGV GGHCIPIDPW FLVENTKAGE FVRLAREIND KRPSIVAEQA
LALLGDTKDN LAGKKVGILG VAYKANVDDC RESPADAILD HFKKAGVDVN YHDPFVPNWH
CEKQETITEI DNWADVLILV TDHECYSNLK VSSLLLNARA
//
