ID B5GZE8_STRCL Unreviewed; 438 AA.
AC B5GZE8;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=GDP-mannose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00020994};
DE EC=1.1.1.132 {ECO:0000256|ARBA:ARBA00012932};
GN ORFNames=SCLAV_5645 {ECO:0000313|EMBL:EFG10712.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG10712.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG10712.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005182}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CM000913; EFG10712.1; -; Genomic_DNA.
DR RefSeq; WP_003957316.1; NZ_WMCA01000111.1.
DR STRING; 1901.BB341_00345; -.
DR GeneID; 61468208; -.
DR KEGG; sclf:BB341_00345; -.
DR eggNOG; COG1004; Bacteria.
DR OrthoDB; 5193947at2; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0047919; F:GDP-mannose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.5.170; -; 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; IPR028358; GDPman_DH.
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 NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43750:SF1; GDP-MANNOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR43750; 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; PIRSF500135; GDPman_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 PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR500135-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EFG10712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 317..424
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-1"
FT BINDING 10
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 161
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 210
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 214
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 217
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 225
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 257
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 259
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 262
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 265
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
FT BINDING 324
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-3"
SQ SEQUENCE 438 AA; 46683 MW; 050A5BFC90D4CBFE CRC64;
MRVSVFGLGY VGCVSAACLA DMGHEVIGVD VNQVKVDLVN SGRAPVVEER IGELVAEAVR
TGALRATGDV GEAIRGSEVS LVCVGTPSEP NGSLCTAYLE RVTEEIGAAL AERGGRQTVV
FRSTMLPGTC LNLLVPILEK SVGGTAGVDF GVAVNPEFLR EGTSVRDFFD PPKTVIGEID
PASGDTVAAL YRDLPGEVFR VPVPTAEAIK YADNAFHGLK IGFANELGAV CQALGVDSHQ
VMDVFLADRK LNISPAYLRP GFAFGGSCLP KDLRSLVHAA HRADVSVPIL AHVLPSNTAH
LQRAVELVER TGRRRAGLFG LSFKPGTDDL RESPLVELAE RLLGKGYDLR IYDANVSLSR
LLGANREYIE TRLPHLAHLL ADSVGEVLEH ADVCLVGTRD PEVLAALPHG EGPVIVDLVR
LPDADRRRAE PGYLGLAW
//
