ALGD_AZOVI
ID ALGD_AZOVI Reviewed; 436 AA.
AC P51585;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=GDP-mannose 6-dehydrogenase;
DE Short=GMD;
DE EC=1.1.1.132;
GN Name=algD;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9046;
RX PubMed=8606150; DOI=10.1128/jb.178.7.1793-1799.1996;
RA Campos M., Martinez-Salazar J.M., Lloret L., Moreno S., Nunez C., Espin G.,
RA Soberon-Chavez G.;
RT "Characterization of the gene coding for GDP-mannose dehydrogenase (algD)
RT 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 is
CC essential for cyst formation.
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; U11240; AAB01487.1; -; Unassigned_DNA.
DR AlphaFoldDB; P51585; -.
DR SMR; P51585; -.
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..436
FT /note="GDP-mannose 6-dehydrogenase"
FT /id="PRO_0000074066"
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 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
