ID   ALGD_PSESY              Reviewed;         438 AA.
AC   P59793;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=GDP-mannose 6-dehydrogenase;
DE            Short=GMD;
DE            EC=1.1.1.132;
GN   Name=algD;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FF5;
RA   Keith R.C., Keith L.M., Bender C.L.;
RT   "Comparative analysis of the algD promoter, gene and protein from
RT   Pseudomonas syringae, Pseudomonas aeruginosa, and Azotobacter vinelandii.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of guanosine diphospho-D-mannose
CC       (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate
CC       polymerization. The alginate layer causes a mucoid phenotype and
CC       provides a protective barrier against host immune defenses and
CC       antibiotics (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AY095347; AAM23311.1; -; Genomic_DNA.
DR   AlphaFoldDB; P59793; -.
DR   SMR; P59793; -.
DR   UniPathway; UPA00286; -.
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   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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52413; SSF52413; 1.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   3: Inferred from homology;
KW   Alginate biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..438
FT                   /note="GDP-mannose 6-dehydrogenase"
FT                   /id="PRO_0000074071"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
FT   SITE            10
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            11
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            30
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            35
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            86
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            161
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            271
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
FT   SITE            331
FT                   /note="NAD binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   438 AA;  47519 MW;  F1A1D44AE37465FE CRC64;
     MRISIFGLGY VGAVCAGCLS ARGHEVVGVD ISSTKIDLIN NGKSPIVEPG LEELLQKGIS
     TGKLRGTTDF AEAIRATDLS MICVGTPSKK NGDLELDYIE SVCREIGYVL RDKATRHTIV
     VRSTVLPGTV ANVVIPILED CSGKKAGVDF GVAVNPEFLR ESTAIKDYDL PPMTVIGEFD
     KASGDVLQSL YEELDAPIIR KDIAVAEMIK YTCNVWHATK VTFANEIGNI AKAVGVDGRE
     VMDVVCQDKA LNLSQYYMRP GFAFGGSCLP KDVRALTYRA GSLDVEAPLL NSLMRSNTSQ
     VQNAFDMVAS YDARKVALLG LSFKAGTDDL RESPLVELAE MLIGKGFDLS IFDSNVEYAR
     VHGANKDYIE SKIPHVSSLL NSDFDQVIND SDVIILGNRD ERFRALANKT PEGKRVIDLV
     GFMANATSED GRAEGICW