ID S6ALD6_PSERE Unreviewed; 436 AA.
AC S6ALD6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 Name=algD {ECO:0000313|EMBL:BAN49555.1};
GN ORFNames=PCA10_38230 {ECO:0000313|EMBL:BAN49555.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN49555.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN49555.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN49555.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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; AP013068; BAN49555.1; -; Genomic_DNA.
DR RefSeq; WP_016493692.1; NC_021499.1.
DR AlphaFoldDB; S6ALD6; -.
DR STRING; 1245471.PCA10_38230; -.
DR KEGG; pre:PCA10_38230; -.
DR PATRIC; fig|1245471.3.peg.3864; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_1_1_6; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00286; -.
DR Proteomes; UP000015503; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
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 436 AA; 47465 MW; 19D8BCCD1C9CD957 CRC64;
MRISIFGLGY VGAVCAGCLS ARGHDIVGVD IAAVKIDMIN QGKSPIVEPG LEELLQQGVA
SGRLRGTLDV REAVLATDIS FIAAPTPSKK NGDLDVSYIA QVCEQISSVL PEKGSRHTVV
VRSTVLPGTV MNVVVPMLER CSGMKAGIDF GVAVNPEFLR ESTAIKDYDY PAMTVIGELD
QTSGDLLQAI YQELDAPIIR KGIEVAEMIK YTCNVWHATK VTFANEIGNI AKAVGVDGRE
VMEVICQDHK LNLSKYYMRP GFAFGGSCLP KDVRALTYRA GQLDIEHPLL HSIMRSNRVQ
VERAFDLIAS HDKRRIGLLG LSFKAGTDDL RESPLVELAE MLIGKGFDLH IFDRNVEYAR
VHGANKDYIE SKIPHVSSLL RSDLDEVVAR ADVIVLGNGD PHFASLVEKV APGKTVVDLV
GFMKERSCAG MEGICW
//