UniProt: C1DP96

Database: UniProt
Entry: C1DP96_AZOVD

LinkDB:  C1DP96_AZOVD 
Original site:  C1DP96_AZOVD

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (8)   
   Pfam (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   C1DP96_AZOVD            Unreviewed;       436 AA.
AC   C1DP96;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=GDP-mannose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00020994, ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.132 {ECO:0000256|ARBA:ARBA00012932, ECO:0000256|PIRNR:PIRNR000124};
GN   Name=algD {ECO:0000313|EMBL:ACO77328.1};
GN   OrderedLocusNames=Avin_10970 {ECO:0000313|EMBL:ACO77328.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO77328.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO77328.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate
CC         + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:21728, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:84886; EC=1.1.1.132;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000124};
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005182, ECO:0000256|PIRNR:PIRNR000124}.
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; CP001157; ACO77328.1; -; Genomic_DNA.
DR   RefSeq; WP_012699749.1; NC_012560.1.
DR   AlphaFoldDB; C1DP96; -.
DR   STRING; 322710.Avin_10970; -.
DR   EnsemblBacteria; ACO77328; ACO77328; Avin_10970.
DR   KEGG; avn:Avin_10970; -.
DR   eggNOG; COG1004; Bacteria.
DR   HOGENOM; CLU_023810_1_1_6; -.
DR   OrthoDB; 9803238at2; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000002424; 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.
PE   3: Inferred from homology;
KW   Alginate biosynthesis {ECO:0000256|ARBA:ARBA00022841,
KW   ECO:0000256|PIRNR:PIRNR000124};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN          317..425
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         256
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   436 AA;  46969 MW;  BE4F275338B4A3DA CRC64;
     MRISIFGLGY VGAVCAGCLS GRGHEVVGVD ISAAKIDMIN QGKSPIVEPG LGELLAEGVK
     TGRLRGTTNV TEAVLATELS MLCVGTPSKL NGDLELDYIE EVCRQMGSAL RDKTERHTVV
     VRSTVLPGTV HNVVIPILEE FSGKKAGVDF GVAVNPEFLR ESTAIKDYNF PPMTVIGELD
     KASGDALASI YAELDAPIVR KDIAVAEMIK YTCNVWHATK VTFANEIGNI AKAAGVDGRE
     VMEVVCMDNK LNLSQYYMRP GFAFGGSCLP KDVSALSYRA HLWDIEAPLI SSLMRSNAAQ
     VQKAYDMIDK HGSRKVALLG LSFKAGTDDL RESPQLELAE MLIGKGFKLS IFDSNVEYAR
     DHGANGHYIK NEIPHVSALL QSDLDKVVAE ADVIVLGNAD PRFEKLAKDV PAGKKVIDLV
     GFMPQRTAGA AEGICW
//

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