ID   ALGD_AZOVI     STANDARD;      PRT;   436 AA.
AC   P51585;
DT   01-OCT-1996 (Rel. 34, Created)
DT   01-OCT-1996 (Rel. 34, 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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 9046;
RX   MEDLINE=96178939; PubMed=8606150;
RA   Campos M., Martinez-Salazar J.M., Lloret L., Moreno S., Nunez C.,
RA   Espin G., Soberon-Chavez G.;
RT   "Characterization of the gene coding for GDP-mannose dehydrogenase
RT   (algD) from Azotobacter vinelandii.";
RL   J. Bacteriol. 178:1793-1799(1996).
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       is essential for cyst formation.
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; U11240; AAB01487.1; -.
DR   HSSP; P11759; 1MV8.
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   436 AA;  47003 MW;  FC9E49347F618677 CRC64;
     MRISIFGLGY VGAVCAGCLS GRGHEVVGVD ISAAKIDMIN QGKSPIVEPG LGELLAEGVK
     TGRLRGTTNV TEAVLATELS MLCVGTPSKL NGDLELDYIE EVCRQMGSAL RDKTERHTVV
     VRSTVLPGTV HNVVIPILEE FSGKKAGVDF GVAVNPEFLR ESTAIKDYNF PPMTVIGELD
     KASGRRLASI YAELDAPIVR KGIAVAEMIK YTCNVWHATK VTFANEIGNI AKAAGVDGRE
     VMEVVCMDNK LNLSQYYMRP GLAFGGSCLP KDVSALSYRA HLWDIEAPLI SSLMRSNAAQ
     VQKAYDMIDK HGSRKVALLG LSFKAGTDDL RESPQLELAE MLIGKGFKLS IFDSNVEYAR
     DHGANGHYIK NEIPHVSALL QSDLDKVVAE ADVIVLGNAD PRFEKLAKDV PAGKKVIDLV
     GFMPQRTAGA AEGICW
//