(data stored in SCRATCH zone)

SWISSPROT: Q144V4_PARXL

ID   Q144V4_PARXL            Unreviewed;       372 AA.
AC   Q144V4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=GDP-mannose 4,6-dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
DE            EC=4.2.1.47 {ECO:0000256|HAMAP-Rule:MF_00955};
DE   AltName: Full=GDP-D-mannose dehydratase {ECO:0000256|HAMAP-Rule:MF_00955};
GN   Name=gmd {ECO:0000256|HAMAP-Rule:MF_00955};
GN   ORFNames=Bxe_A3863 {ECO:0000313|EMBL:ABE29135.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29135.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29135.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29135.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-
CC       dehydro-6-deoxy-D-mannose. {ECO:0000256|HAMAP-Rule:MF_00955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose +
CC         H2O; Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57964; EC=4.2.1.47; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00955};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00955};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00955}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00955}.
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DR   EMBL; CP000270; ABE29135.1; -; Genomic_DNA.
DR   RefSeq; WP_007179059.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3863; -.
DR   EnsemblBacteria; ABE29135; ABE29135; Bxe_A3863.
DR   GeneID; 4002484; -.
DR   KEGG; bxb:DR64_1539; -.
DR   KEGG; bxe:Bxe_A3863; -.
DR   eggNOG; ENOG4105C0K; Bacteria.
DR   eggNOG; COG1089; LUCA.
DR   HOGENOM; HOG000168003; -.
DR   KO; K01711; -.
DR   OMA; FVKSSWQ; -.
DR   OrthoDB; 955232at2; -.
DR   BioCyc; BXEN266265:BXE_RS02950-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:InterPro.
DR   HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR   InterPro; IPR006368; GDP_Man_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01472; gmd; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q144V4.
DR   SWISS-2DPAGE; Q144V4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00955, ECO:0000313|EMBL:ABE29135.1};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        7    346       NAD(P)-bd_dom. {ECO:0000259|Pfam:
FT                                PF16363}.
SQ   SEQUENCE   372 AA;  42136 MW;  5B4E7D6E4A856A3A CRC64;
     MKRKVALITG ITGQDGSYLA ELLLAKDYDV HGIKRRSSLF NTDRIDHLYR DPHDPDQRLF
     LHHADLTDST SILRVIQRVE PDEIYNLAAQ SHVAVSFEEP EYTANADGLG ALRILEAIRI
     LGLQEKTRFY QASTSELYGL VQQVPQSETT PFYPRSPYAV AKLFAYWTTV NYREAYGLYA
     CNGILFNHES PVRGETFVTR KITRAVARIA VGMQKTLYLG NLSALRDWGH ARDYVEMQWR
     MLQQEQPEDY VIATGVQYSV RQFVQHAAAE LGVTVRFEGT GVDEIGIVEK VEGREIKMSP
     GDVIVRVDPR YFRPAEVETL LGDPSKAHAK LGWQPTTSFA SLVKEMVRAD YQIARRDALV
     TLAGFTALEH HE
//

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