ID ALGD_PSESH Reviewed; 438 AA.
AC O07299;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=GDP-mannose 6-dehydrogenase;
DE Short=GMD;
DE EC=1.1.1.132;
GN Name=algD;
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S2-1;
RA Koopmann B., Noellenburg M., Rudolph K.;
RT "Isolation and characterization of the algD gene from Pseudomonas syringae
RT pv. phaseolicola and distribution among other pseudomonads and related
RT organisms.";
RL Submitted (APR-1997) 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). {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; AF001555; AAB58939.1; -; Genomic_DNA.
DR RefSeq; WP_002552256.1; NZ_RBUR01000168.1.
DR AlphaFoldDB; O07299; -.
DR SMR; O07299; -.
DR GeneID; 69858106; -.
DR PATRIC; fig|319.14.peg.1298; -.
DR OMA; GSLCTTY; -.
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 Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43750:SF1; GDP-MANNOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 3: Inferred from homology;
KW Alginate biosynthesis; NAD; Oxidoreductase.
FT CHAIN 1..438
FT /note="GDP-mannose 6-dehydrogenase"
FT /id="PRO_0000074069"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 161
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 210
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 214
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 217
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 225
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 256
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 257
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 259
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 262
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 265
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 324
FT /ligand="GDP-alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:84886"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P11759"
SQ SEQUENCE 438 AA; 47595 MW; 6A4EDC8BC55BCC8F CRC64;
MRISIFGLGY VGAVCAGCLS ARGHDVVGVD 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 SSLDVEAPLL NSLMRSNTSQ
VQNAFDMVAS YDTRKVALLG LSFKAGTDDL RESPLVELAE MLIGKGFDLS IFDSNVEYAR
VHGANKDYIE SKIPHVSSLL NSDFDQVIND SDVIILGNRD ERFRALANKT PEGKRVIDLV
GFMTNATSED GRAEGICW
//
