GenomeNet

Database: UniProt
Entry: A0A151CHG5_9PROT
LinkDB: A0A151CHG5_9PROT
Original site: A0A151CHG5_9PROT 
ID   A0A151CHG5_9PROT        Unreviewed;       397 AA.
AC   A0A151CHG5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   18-SEP-2019, entry version 25.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=AS592_00305 {ECO:0000313|EMBL:KYJ86985.1};
OS   Sulfurovum riftiae.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=1630136 {ECO:0000313|EMBL:KYJ86985.1, ECO:0000313|Proteomes:UP000075359};
RN   [1] {ECO:0000313|EMBL:KYJ86985.1, ECO:0000313|Proteomes:UP000075359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1812E {ECO:0000313|EMBL:KYJ86985.1,
RC   ECO:0000313|Proteomes:UP000075359};
RA   Vetriani C., Giovannelli D.;
RT   "Draft genome of Sulfurovum riftiae 1812E, a member of the
RT   Epsilonproteobacteria isolated from the tube of the deep-sea
RT   hydrothermal vent tubewom Riftia pachyptila.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH +
CC         UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885;
CC         EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYJ86985.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LNKT01000009; KYJ86985.1; -; Genomic_DNA.
DR   RefSeq; WP_067329698.1; NZ_LNKT01000009.1.
DR   EnsemblBacteria; KYJ86985; KYJ86985; AS592_00305.
DR   BioCyc; GCF_001595645:AS592_RS04185-MONOMER; -.
DR   Proteomes; UP000075359; Unassembled WGS sequence.
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:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
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; 2.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075359};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      308    395       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   REGION      142    145       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   REGION      242    246       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   ACT_SITE    253    253       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      29     29       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      34     34       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      83     83       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     118    118       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     145    145       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     197    197       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     250    250       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     256    256       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     314    314       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     315    315       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     322    322       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     396    396       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
SQ   SEQUENCE   397 AA;  44405 MW;  6219CA2E7CB6CF8F CRC64;
     MKIAIAGTGY VGLSNGILLA QHNEVVALDI VPEKVEMLNA KHSPIEDREI EEYLQTKELN
     FRATLDKEEA YKGANFVIIS TPTDYDPETN YFNTKSVEAV IQDVLAVNPD AVMVIKSTVP
     VGYTKSVREK FETENIIFSP EFLREGSALY DNLYPSRIIV GEKSEGAETF AELLKQGALK
     EDIPVLFTDS TEAEAIKLFS NTYLAMRVAY FNELDSYAES HGLDSRQIIE GVGLDPRIGD
     HYNNPSFGYG GYCLPKDTKQ LLANYKDVPS NIIEAIVNAN STRKDFIADQ IIARLPKDAH
     GFPTGIVGVY RLVMKSGSDN FRASAIQGIM KRIKAKGIEV VIYEPVLEED EFFHSKVIKN
     LDEFKKISNV IVANRLSENL KDIEDKVYTR DIFNSDS
//
DBGET integrated database retrieval system