ID   ALGD_PSESY     STANDARD;      PRT;   438 AA.
AC   P59793;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
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.
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.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AY095347; AAM23311.1; -.
DR   InterPro; IPR008927; 6DGDH_C_like.
DR   InterPro; IPR001732; UDPG_MGDP_dh.
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   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   ACT_SITE    268    268       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
//