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 13-SEP-2023, entry version 98. DE RecName: Full=GDP-mannose 6-dehydrogenase; DE Short=GMD; DE EC=1.1.1.132; GN Name=algD; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadota; 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}. 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; 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 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..436 FT /note="GDP-mannose 6-dehydrogenase" FT /id="PRO_0000074066" 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 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 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 //