GenomeNet

Database: UniProt/TrEMBL
Entry: D4ZDT0_SHEVD
LinkDB: D4ZDT0_SHEVD
Original site: D4ZDT0_SHEVD 
ID   D4ZDT0_SHEVD            Unreviewed;       877 AA.
AC   D4ZDT0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:BAJ03991.1};
GN   OrderedLocusNames=SVI_4020 {ECO:0000313|EMBL:BAJ03991.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ03991.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011177; BAJ03991.1; -; Genomic_DNA.
DR   RefSeq; WP_013053282.1; NC_014012.1.
DR   STRING; 637905.SVI_4020; -.
DR   EnsemblBacteria; BAJ03991; BAJ03991; SVI_4020.
DR   KEGG; svo:SVI_4020; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002350; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002350};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:BAJ03991.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    545    545       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   877 AA;  99058 MW;  9881B6AF89708819 CRC64;
     MTDMYASLRS NVGTLGQILG ETIRTNLDDA FLDKIEQIRQ LAKSSRQGDE ASREEMLKLL
     AALPDNELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVEQLLG RVLSSNIDQE
     DMLDCLQNLD IDLVLTAHPT EISRRTLIQK YSSVIDSLAA LENPQLTERE KKQQHLRLRQ
     LIAQIWHTNE IRHERPTPVD EARWGLSTIE VSLWQAIPDF LRQLNEQVEE RTGKQLPIDI
     SPVRFSSWMG GDRDGNPFVT ALVTQEVLDR NRHTAARLYL KDIVLLVNDL SMEDANDELS
     SLTKDSHEPY RYVLRELRVK LRNTIDYLND RLEGHNPKVD NSTIIWHEKD LKEPLMMLYR
     SLSDKGMSLI ANGLLLDMLR RIACFGIHML RLDIRQDAER HSDVIAELTR YLGMGDFNHW
     DESEKQTFLL KELTSKRPLI PTNWQPSDNV AEVISTCRLI ATQPARALGS YVISMASKPS
     DVLTVLLLLK ETGCPHPMRV VPLFETLDDL NNAATCMSAL FAIDWYRGYT KGHQEIMIGY
     SDSAKDAGVM AAAWAQYHAQ EQLVEISRQA DVKLTLFHGR GGTIGRGGGP AHEAILSQPP
     GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPEPKP EWRACIQRLA
     EESVKAYRSI VREEADFVAY FRAATPEVEL GKLPLGSRPA KRKVDGGIES LRAIPWIFAW
     SQNRLMLPAW LGAGEALQAS IDRGDMSLLQ EMEQEWPFFK TRISMLEMVY SKAEPNLAKY
     YETCLVPENL HHLGEALRER LATGIKAVLE LTQSDTLMSH TPWNKESITL RNPYIDPLNF
     MQAELLARTR KEDASANVEL ALMLTIAGVA AGMRNTG
//
DBGET integrated database retrieval system