ID A0A1V9UVC8_9PSED Unreviewed; 438 AA.
AC A0A1V9UVC8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=BWR59_09720 {ECO:0000313|EMBL:OQR33601.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR33601.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR33601.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR33601.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR33601.1}.
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DR EMBL; MUIN01000005; OQR33601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9UVC8; -.
DR STRING; 1943632.BWR59_09720; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000192462; Unassembled WGS sequence.
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 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 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 438 AA; 47201 MW; 50FEB61ACB13C8E6 CRC64;
MHISIFGLGY VGAVCAGCLS ARGHDVVGVD ISSAKIDLIN KGKSPIVEPG LGELLETGIK
TGKLRGTTDF SEAIRATDLS MICVGTPSKK NGDLELDFIE SVCREIGFVL RDKTSRHTIV
VRSTVLPGTV ANVVIPILED CSGKKAGVDF GVAVNPEFLR ESTAIADYDH PPMTVIGEFD
KASGDVLQSL YEELDAPIIR KDIAVAEMIK YTCNVWHATK VTFANEIGNI AKAVGVDGRE
VMEVVCQDKA LNLSQYYMRP GFAFGGSCLP KDVRALTYRA STLDVEAPLL NSLMRSNVSQ
VQNAFDIVAA TDTRKVALLG LSFKAGTDDL RESPLVELAE MLIGKGFDLS IFDSNVEYAR
VHGANKDYIE SKIPHVSSLL NSDFDAVIDN SDVIILGNRD ERFRALANNA PAGKKVIDLV
GFMTGTTTEN GQTEGICW
//
