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Database: UniProt
Entry: B6WAF2_9FIRM
LinkDB: B6WAF2_9FIRM
Original site: B6WAF2_9FIRM 
ID   B6WAF2_9FIRM            Unreviewed;       489 AA.
AC   B6WAF2;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=ANHYDRO_01580 {ECO:0000313|EMBL:EEB35592.1};
OS   Anaerococcus hydrogenalis DSM 7454.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=561177 {ECO:0000313|EMBL:EEB35592.1, ECO:0000313|Proteomes:UP000005451};
RN   [1] {ECO:0000313|EMBL:EEB35592.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB35592.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB35592.1, ECO:0000313|Proteomes:UP000005451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB35592.1,
RC   ECO:0000313|Proteomes:UP000005451};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000874,
CC         ECO:0000256|PIRNR:PIRNR000124};
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:0000256|ARBA:ARBA00004701}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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:EEB35592.1}.
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DR   EMBL; ABXA01000041; EEB35592.1; -; Genomic_DNA.
DR   RefSeq; WP_004814974.1; NZ_ABXA01000041.1.
DR   AlphaFoldDB; B6WAF2; -.
DR   STRING; 561177.ANHYDRO_01580; -.
DR   eggNOG; COG1004; Bacteria.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000005451; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_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   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750:SF2; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   Pfam; PF01381; HTH_3; 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; PIRSF500134; UDPglc_DH_bac; 2.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN          13..67
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         225..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         328..332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         342
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         417
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ   SEQUENCE   489 AA;  55275 MW;  012BCAF521F69492 CRC64;
     MKKLSVEKLA DFVSTYRKSK NFSQRNLSDL TGINRTMISR IESCDYVPSI DQLQALAEVL
     GFDIVDLFVE EGKKSFMKNI DKKYKIAVAG TGYVGLSIAT LLAQNNQVTA VDIVKEKVDL
     INERKSPIQD DYIEKYLREK DLDLTATLDG EAAYRDADFV VIAAPTNYDS KKNFFDCSAV
     ESVIELVLKV NPSATMIIKS TIPVGYTKSV REKYNTKNII FSPEFLRESK ALYDNLYPSR
     IIVSCDDESR ERAEIFASLL QEGAIKENID TLFMGFTEAE AVKLFANTYL ALRVSYFNEL
     DTYAESKGLN TEEIINGVCL DPRIGSHYNN PSFGYGGYCL PKDTKQLLAN FDKVPQNMIS
     AIVDANSTRK DFIADQVLNI AGYYSYNEDV QYRPEKEKEC VIGVYRLTMK SNSDNFRQSS
     IQGVMKRIKA KGATVIIYEP TLKDGQTFFG SEVVNNLKKF KKMSQAIIAN RYDACLDDVI
     DKVYTRDIF
//
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