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Database: UniProt
Entry: S2KCE3_9PSED
LinkDB: S2KCE3_9PSED
Original site: S2KCE3_9PSED 
ID   S2KCE3_9PSED            Unreviewed;       438 AA.
AC   S2KCE3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   05-DEC-2018, entry version 23.
DE   RecName: Full=GDP-mannose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.132 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=L321_23566 {ECO:0000313|EMBL:EPB93188.1};
OS   Pseudomonas plecoglossicida NB2011.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1330531 {ECO:0000313|EMBL:EPB93188.1, ECO:0000313|Proteomes:UP000014440};
RN   [1] {ECO:0000313|EMBL:EPB93188.1, ECO:0000313|Proteomes:UP000014440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NB2011 {ECO:0000313|EMBL:EPB93188.1,
RC   ECO:0000313|Proteomes:UP000014440};
RX   PubMed=23929479;
RA   Mao Z., Li M., Chen J.;
RT   "Draft Genome Sequence of Pseudomonas plecoglossicida Strain NB2011,
RT   the Causative Agent of White Nodules in Large Yellow Croaker
RT   (Larimichthys crocea).";
RL   Genome Announc. 1:e00586-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-
CC         mannuronate + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:21728,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:84886;
CC         EC=1.1.1.132; Evidence={ECO:0000256|PIRNR:PIRNR000124};
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR000124}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPB93188.1}.
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DR   EMBL; ASJX01000087; EPB93188.1; -; Genomic_DNA.
DR   RefSeq; WP_016395472.1; NZ_KE166455.1.
DR   EnsemblBacteria; EPB93188; EPB93188; L321_23566.
DR   PATRIC; fig|1330531.3.peg.4632; -.
DR   UniPathway; UPA00286; -.
DR   Proteomes; UP000014440; 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   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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52413; SSF52413; 1.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   3: Inferred from homology;
KW   Alginate biosynthesis {ECO:0000256|PIRNR:PIRNR000124};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014440};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500135-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      317    425       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   NP_BIND       7     12       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   REGION      157    161       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500135-2}.
FT   REGION      210    217       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500135-2}.
FT   REGION      256    265       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500135-2}.
FT   ACT_SITE    268    268       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500135-1}.
FT   BINDING      30     30       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING      35     35       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING      86     86       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING     105    105       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING     124    124       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING     271    271       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
FT   BINDING     331    331       NAD. {ECO:0000256|PIRSR:PIRSR500135-3}.
SQ   SEQUENCE   438 AA;  47780 MW;  15BBCA01EA44C079 CRC64;
     MRISIFGLGY VGAVCAGCLT ARGHDVIGVD VSKTKIDLIN QGKSPIVEPG LEALLQQGIA
     NGRLRGTTDF AEAIRASDVS MICVGTPSKK NGDLGLEYIE SVCREIGYVL RDTTRRHTIV
     VRSTVLPGTV KNVVIPILED CSGKKAGVDF GVAVNPEFLR ESTAIKDYDH PPMTVIGELD
     SASGDVLQSL YEELDAPVIR KPIEVAEMIK YTCNVWHATK VTFANEIGNI AKAVGVDGRD
     VMDVVCQDKV LNLSQYYMRP GFAFGGSCLP KDVRALSYRA ASLDVRAPLL DSLMRSNESQ
     VQNAFELIEA HDKRKVALLG LSFKAGTDDL RESPLVELAE RLIGKGYQLD IYDENVEYAR
     VHGANKDYIE SKIPHVSSLL NADFQKVIDN ADIIVLGNRD EQFRALAQQA PAGKQVIDLV
     GFMSKPTCTT SRTEGICW
//
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