ID   ALGD_PSEPK              Reviewed;         438 AA.
AC   Q88NC4;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=GDP-mannose 6-dehydrogenase;
DE            Short=GMD;
DE            EC=1.1.1.132;
GN   Name=algD; OrderedLocusNames=PP_1288;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66912.1; -; Genomic_DNA.
DR   RefSeq; NP_743448.1; NC_002947.4.
DR   RefSeq; WP_010952417.1; NC_002947.4.
DR   AlphaFoldDB; Q88NC4; -.
DR   SMR; Q88NC4; -.
DR   STRING; 160488.PP_1288; -.
DR   EnsemblBacteria; AAN66912; AAN66912; PP_1288.
DR   KEGG; ppu:PP_1288; -.
DR   PATRIC; fig|160488.4.peg.1365; -.
DR   eggNOG; COG1004; Bacteria.
DR   HOGENOM; CLU_023810_1_1_6; -.
DR   OMA; KYADNAF; -.
DR   PhylomeDB; Q88NC4; -.
DR   BioCyc; PPUT160488:G1G01-1375-MON; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000000556; 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   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; Reference proteome.
FT   CHAIN           1..438
FT                   /note="GDP-mannose 6-dehydrogenase"
FT                   /id="PRO_0000074068"
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;  47728 MW;  51CEBCDBEE95B748 CRC64;
     MRISIFGLGY VGAVCAGCLT ARGHEVIGVD VSSTKIDLIN QGKSPIVEPG LEALLQQGIA
     NGRLRGTTDF AEAIRASDVS MICVGTPSKK NGDLGLEYIE SVCREIGYVL RDTTRRHTIV
     VRSTVLPGTV KNVVIPILED CSGKKAGVDF GVAVNPEFLR ESTAIKDYDQ PPMTVIGELD
     SASGDILQAL YEELDAPIIR KPIEVAEMIK YTCNVWHATK VTFANEIGNI AKAVGVDGRE
     VMDVVCQDKV LNLSQYYMRP GFAFGGSCLP KDVRALTYRA ASLDVRAPLL DSLMRSNESQ
     VQNAFELIEA HDKRKVALLG LSFKAGTDDL RESPLVELAE RLIGKGYQLD IYDENVQYAR
     VHGANKDYIE SKIPHVSSLL NANLQQVIDN ADIIVLGNRD EQFRALALQA PAGKQVIDLV
     GFMNKPTSTT ARTEGICW