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Database: UniProt
Entry: C2GDW9_9CORY
LinkDB: C2GDW9_9CORY
Original site: C2GDW9_9CORY 
ID   C2GDW9_9CORY            Unreviewed;       440 AA.
AC   C2GDW9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN   Name=rkpK {ECO:0000313|EMBL:EEI64412.1};
GN   ORFNames=HMPREF0293_0130 {ECO:0000313|EMBL:EEI64412.1};
OS   Corynebacterium glucuronolyticum ATCC 51866.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=548478 {ECO:0000313|EMBL:EEI64412.1, ECO:0000313|Proteomes:UP000006237};
RN   [1] {ECO:0000313|EMBL:EEI64412.1, ECO:0000313|Proteomes:UP000006237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51866 {ECO:0000313|EMBL:EEI64412.1,
RC   ECO:0000313|Proteomes:UP000006237};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) 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:EEI64412.1}.
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DR   EMBL; ACHF01000008; EEI64412.1; -; Genomic_DNA.
DR   RefSeq; WP_005393424.1; NZ_GG667032.1.
DR   AlphaFoldDB; C2GDW9; -.
DR   HOGENOM; CLU_023810_1_2_11; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000006237; 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   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 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; 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; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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; 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.
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          322..423
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT   BINDING         30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         153..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         255..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT   BINDING         336
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ   SEQUENCE   440 AA;  46927 MW;  36272F30CB2C0581 CRC64;
     MKMTVIGTGY LGATHAACMA ELGHEVCGVD VDESKIAALA SGQVPFFEPG LPEILTRTVS
     SGRLSFTTSY EEAANFAHVH FLGVGTPQMH GSYAADLTYV HAAIDTLVPL LRGAHIIFGK
     STVPVGTAAD LQARADRLAP EGTHVEIVWN PEFLREGFAV TDTISPDRIV LGTASPDSPA
     IDVAREIYAQ PLSQGTPLIV TNLPTAELVK VSANSFLATK ISFINAVSEI CEVTGADVVK
     LAEAIGYDDR IGKKFLRAGL GFGGGCLPKD IRAFMARAGE LGASEALSFL REVDSINMRR
     REHVVELSKL LCDGSLLGKN ITVLGAAFKP NSDDVRDSPA LSVAGSLSLK GANVTVYDPE
     AMDNAARVFP TLDYAQNVND ALSGADLTIL ATEWDEFRQL DPEKAGDLVN RRVMLDARNV
     LHTSDWCEKG WQVKALGCGE
//
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