ID   ALGD_PSESY     STANDARD;      PRT;   438 AA.
AC   P59793;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 1.
DT   21-MAR-2006, entry version 15.
DE   GDP-mannose 6-dehydrogenase (EC 1.1.1.132) (GMD).
GN   Name=algD;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
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
RT   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).
CC   -!- CATALYTIC ACTIVITY: GDP-D-mannose + 2 NAD(+) + H(2)O = GDP-D-
CC       mannuronate + 2 NADH.
CC   -!- PATHWAY: Alginate biosynthesis; fourth step.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; AY095347; AAM23311.1; -; Genomic_DNA.
DR   SMR; P59793; 1-438.
DR   InterPro; IPR008927; 6DGDH_C_like.
DR   InterPro; IPR001732; UDPG_MGDP_DH.
DR   PANTHER; PTHR11374; UDPG_MGDP_dh; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
KW   Alginate biosynthesis; NAD; Oxidoreductase.
FT   CHAIN         1    438       GDP-mannose 6-dehydrogenase.
FT                                /FTId=PRO_0000074071.
FT   ACT_SITE    268    268       By similarity.
FT   SITE         10     10       NAD binding (By similarity).
FT   SITE         11     11       NAD binding (By similarity).
FT   SITE         30     30       NAD binding (By similarity).
FT   SITE         35     35       NAD binding (By similarity).
FT   SITE         86     86       NAD binding (By similarity).
FT   SITE        161    161       NAD binding (By similarity).
FT   SITE        271    271       NAD binding (By similarity).
FT   SITE        331    331       NAD binding (By similarity).
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
//