ID A4XSX6_PSEMY Unreviewed; 436 AA.
AC A4XSX6;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=GDP-mannose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00020994, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.132 {ECO:0000256|ARBA:ARBA00012932, ECO:0000256|PIRNR:PIRNR000124};
GN OrderedLocusNames=Pmen_1678 {ECO:0000313|EMBL:ABP84442.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84442.1};
RN [1] {ECO:0000313|EMBL:ABP84442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP84442.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|PIRNR:PIRNR000124};
CC -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005182, ECO:0000256|PIRNR:PIRNR000124}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP000680; ABP84442.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XSX6; -.
DR STRING; 399739.Pmen_1678; -.
DR KEGG; pmy:Pmen_1678; -.
DR PATRIC; fig|399739.8.peg.1700; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_1_1_6; -.
DR OrthoDB; 9803238at2; -.
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 {ECO:0000256|ARBA:ARBA00022841,
KW ECO:0000256|PIRNR:PIRNR000124};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124}.
FT DOMAIN 317..425
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-1"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-3"
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:0000256|PIRSR:PIRSR500135-2"
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:0000256|PIRSR:PIRSR500135-2"
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:0000256|PIRSR:PIRSR500135-2"
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:0000256|PIRSR:PIRSR500135-2"
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:0000256|PIRSR:PIRSR500135-2"
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 A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
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 A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
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 A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
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 A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 271
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:0000256|PIRSR:PIRSR500135-3"
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 A"
FT /evidence="ECO:0000256|PIRSR:PIRSR500135-2"
FT BINDING 331
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:0000256|PIRSR:PIRSR500135-3"
SQ SEQUENCE 436 AA; 47111 MW; 7BD23B87A4C67AA8 CRC64;
MRITIFGLGY VGAVCAGCLS ARGHEVIGVD VSQTKIDLIN QGKSPIVEPG LAELLEAGVN
SGRLRGTTDV AAAVMASELS FIAVGTPSKR NGDLDLGYME SVCKQIGAAL RDKQDRHTVV
VRSTVLPGTV KNVVIPLIEA ASGKKAGVDF GVATNPEFLR ESTAIKDYDF PAMTVIGELD
QQSGDLLQEL YSELDAPIIR KSIEVAEMIK YTCNVWHAAK VTFANEIGNI AKAAGVDGRE
VMDVVCQDHK LNLSKYYMKP GFAFGGSCLP KDVRALSYRA GSLDVDAPLI GSLMRSNAAQ
VKKAFDIVAN YDKRRIGLLG LSFKAGTDDL RESPLVELAE MLIGKGYELR IFDSNVEYAR
VFGANKEYIE SKIPHVSSLL CKELDEVVAQ SDVLIIGNGE QRFAEVMDSI GDDKQIVDLV
GFMAHPTQAN REGICW
//
