ID ALGD_PSESY Reviewed; 438 AA. AC P59793; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 1. DT 13-SEP-2023, entry version 77. DE RecName: Full=GDP-mannose 6-dehydrogenase; DE Short=GMD; DE EC=1.1.1.132; GN Name=algD; OS Pseudomonas syringae pv. syringae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae. 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 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). {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY095347; AAM23311.1; -; Genomic_DNA. DR AlphaFoldDB; P59793; -. DR SMR; P59793; -. 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_0000074071" 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; 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 //