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Database: UniProt/TrEMBL
Entry: A4YBU3_SHEPC
LinkDB: A4YBU3_SHEPC
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ID   A4YBU3_SHEPC            Unreviewed;       889 AA.
AC   A4YBU3;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   22-NOV-2017, entry version 78.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Sputcn32_3718 {ECO:0000313|EMBL:ABP77426.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP77426.1, ECO:0000313|Proteomes:UP000006699};
RN   [1] {ECO:0000313|EMBL:ABP77426.1, ECO:0000313|Proteomes:UP000006699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453 {ECO:0000313|Proteomes:UP000006699};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Romine M.F., Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP000681; ABP77426.1; -; Genomic_DNA.
DR   RefSeq; WP_011920204.1; NC_009438.1.
DR   STRING; 319224.Sputcn32_3718; -.
DR   EnsemblBacteria; ABP77426; ABP77426; Sputcn32_3718.
DR   KEGG; spc:Sputcn32_3718; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006699; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006699};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABP77426.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABP77426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006699}.
FT   ACT_SITE    146    146       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    553    553       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   889 AA;  100366 MW;  9BEBDBABBEE47793 CRC64;
     MSVNAADNMT DMYASLRSNV SMLGQILGDT MRTHLGDSFL EKVEQIRKLA KDSRRGDQAA
     REQMLELLTA LPDEELVPFA KAFNQFLNLA NLSEQFHTIS RNCDELVCVP DPVEQLLGRM
     LNGRIDQTKM LDCLKTLDID LVLTAHPTEI SRRTLIQKYA AIVDCLTEQE NDQLSDRERQ
     QINLRLRQLI AQIWHTNEIR RERPTPVDEA RWGLSTIEES LWHAVPDFLR QLNDQVQQRT
     GQQLPIDIAP VRFSSWMGGD RDGNPFVTAK VTQEVLDRNR HAAARLFLKD IVLLVGELSM
     EEANDELKAY TNNNCEPYRH VLRSLRQRLR DTIDYLNARI EGHNPEVDKS SLIWQESDLK
     VPLEMLYKSL TDCGMRLIAN GLLLDILRRL ACFGIHMLRL DIRQDASRHS DVLAELTRYL
     GMGDFNHWDE TEKQAFLLRE LSNRRPLIPS NWQPSADVAE VLNTCRLIAK HPAKALGSYV
     ISMAGKPSDV LTVLLLLKET GCSHPMRVVP LFETLSDLNN AAACITDLLD IDWYRGYTKG
     MQEVMIGYSD SAKDAGVMAA AWAQYRAQEQ LVAVCKQAGV KLTLFHGRGG SIGRGGGPAH
     KAILSQPPGS VDGRIRVTEQ GEMIRFKFGL PKLAVQSLAL YTSAVLEATL LPPPEPKQEW
     RNCMQRIAEE SVGAYRGIVR DEPDFVAYFR AATPEVELGK LPLGSRPAKR RVDGGIESLR
     AIPWIFAWSQ NRLMLPAWLG AGEALQAASE RGEMGLLQDM EREWPFFSTR ISMLEMVYAK
     AEPNLARYYE TCLVPKDLHH LGETLRQRLD LGIKVVLELT KSDSLMAHTP WNRESVKLRN
     PYIDPLNFLQ TELLARTRKE TTETPASEHV QLALMLTIAG VAAGMRNTG
//
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