UDG_RHIME
ID UDG_RHIME Reviewed; 437 AA.
AC O54068;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000305};
DE Short=UDP-Glc dehydrogenase {ECO:0000305};
DE Short=UDP-GlcDH {ECO:0000305};
DE Short=UDPGDH {ECO:0000305};
DE EC=1.1.1.22 {ECO:0000269|PubMed:9765575};
GN Name=rkpK {ECO:0000303|PubMed:9765575}; OrderedLocusNames=R01082;
GN ORFNames=SMc02641;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=41;
RX PubMed=9765575; DOI=10.1128/jb.180.20.5426-5431.1998;
RA Kereszt A., Kiss E., Reuhs B.L., Carlson R.W., Kondorosi A., Putnoky P.;
RT "Novel rkp gene clusters of Sinorhizobium meliloti involved in capsular
RT polysaccharide production and invasion of the symbiotic nodule: the rkpK
RT gene encodes a UDP-glucose dehydrogenase.";
RL J. Bacteriol. 180:5426-5431(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000269|PubMed:9765575};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000305}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:9765575}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ222661; CAA10918.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45661.1; -; Genomic_DNA.
DR PIR; T46573; T46573.
DR RefSeq; NP_385188.1; NC_003047.1.
DR RefSeq; WP_010969031.1; NC_003047.1.
DR AlphaFoldDB; O54068; -.
DR SMR; O54068; -.
DR STRING; 266834.SMc02641; -.
DR EnsemblBacteria; CAC45661; CAC45661; SMc02641.
DR GeneID; 61602542; -.
DR KEGG; sme:SMc02641; -.
DR PATRIC; fig|266834.11.peg.2490; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_1_2_5; -.
DR OMA; CECLNLP; -.
DR UniPathway; UPA00038; UER00491.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR028357; UDPglc_DH_bac.
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; PIRSF500134; UDPglc_DH_bac; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..437
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074050"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 254..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT BINDING 333
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT CONFLICT 109
FT /note="A -> S (in Ref. 1; CAA10918)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> V (in Ref. 1; CAA10918)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> Y (in Ref. 1; CAA10918)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> T (in Ref. 1; CAA10918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 47122 MW; 2D458D39A1D8EEC1 CRC64;
MKITMIGAGY VGLVSGVCFA DFGHDVVCVD KDEGKISALK KGQIPIFEPG LDHLVASNVA
SGRLNFTDDL KTAVAASDVV FIAVGTPSRR GDGHADLSYV YAAAREIAAN LQGFTVVVTK
STVPVGTGDE VERIIRETNP AADVTVVSNP EFLREGAAIE DFKRPDRIVI GVDGSDGRAR
EVMTEVYRPL YLNQSPLVFT TRRTSELIKY AGNAFLAMKI TFINEIADLC EKVGANVQDV
ARGIGLDGRI GSKFLHAGPG YGGSCFPKDT LALVKTAQDH DTPVRLVETT VAVNDNRKRA
MGRKVIAAAG GDIRGSKIAV LGLTFKPNTD DMRDSPAIAV VQALQDAGAR VTGYDPEGME
NARKLIEGLD CARDPYEAAA EADALVIITE WNEFRALDFD RLKSTMKTPL LVDLRNIYRK
DEVAKHGFRY ASIGRPD
