ID   ALGD_PSESH              Reviewed;         438 AA.
AC   O07299;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=GDP-mannose 6-dehydrogenase;
DE            Short=GMD;
DE            EC=1.1.1.132;
GN   Name=algD;
OS   Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS   phaseolicola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S2-1;
RA   Koopmann B., Noellenburg M., Rudolph K.;
RT   "Isolation and characterization of the algD gene from Pseudomonas syringae
RT   pv. phaseolicola and distribution among other pseudomonads and related
RT   organisms.";
RL   Submitted (APR-1997) 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; AF001555; AAB58939.1; -; Genomic_DNA.
DR   RefSeq; WP_002552256.1; NZ_RBUR01000168.1.
DR   AlphaFoldDB; O07299; -.
DR   SMR; O07299; -.
DR   GeneID; 61868476; -.
DR   PATRIC; fig|319.14.peg.1298; -.
DR   OMA; KYADNAF; -.
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_0000074069"
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;  47595 MW;  6A4EDC8BC55BCC8F CRC64;
     MRISIFGLGY VGAVCAGCLS ARGHDVVGVD 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 SSLDVEAPLL NSLMRSNTSQ
     VQNAFDMVAS YDTRKVALLG LSFKAGTDDL RESPLVELAE MLIGKGFDLS IFDSNVEYAR
     VHGANKDYIE SKIPHVSSLL NSDFDQVIND SDVIILGNRD ERFRALANKT PEGKRVIDLV
     GFMTNATSED GRAEGICW