ID   Q089L3_SHEFN            Unreviewed;       882 AA.
AC   Q089L3;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
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|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
DE   Flags: Precursor;
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Sfri_0189 {ECO:0000313|EMBL:ABI70052.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70052.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI70052.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70052.1,
RC   ECO:0000313|Proteomes:UP000000684};
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., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP000447; ABI70052.1; -; Genomic_DNA.
DR   RefSeq; WP_011635679.1; NC_008345.1.
DR   AlphaFoldDB; Q089L3; -.
DR   STRING; 318167.Sfri_0189; -.
DR   KEGG; sfr:Sfri_0189; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000684; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ABI70052.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684}.
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        549
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   882 AA;  99486 MW;  A2C9F5D321650745 CRC64;
     MTEQTADMYA SLRSNVGHLG QILGETMQNH LGDAFLEKVE QIRILAKKSR QGDEASREQM
     LALLTALPDE ELVPFAKAFN QFLNLANIAE QFHTISRNCD ELVCVPDPVE QLLGRMLDTD
     LDKKDVIKSL KNLDIDLVLT AHPTEISRRT LIQKYAAVVD CLTEQENSQL TDRERQQSTL
     RLRQLIAQIW HTNEIRNERP TPVDEARWGL STIETSLWQA IPDFLRQLND QVEQKTGQQL
     PIDVSPVRFS SWMGGDRDGN PFVTSLVTQE VLDRNRHAAA RLYLKDIVSL LGELSMEQAN
     AELSALTDNS KEPYRDVLRK LRCQLHGTID YLNARLEGKK PDVDTSELIW HKSDLLEPLE
     LLYKSLTDCG MKLIANGLLL DILRRLACFG IHMLRLDIRQ DATRHSDVIA ELTRYLGMGD
     YNHWDENEKQ AFLLRELTSK RPLIPTNWKP TDDVAEVVRT CNLVAQQPVN ALGSYVISMA
     SKPSDVLTVL LLLKEAGCTN PMRVVPLFET LADLEGAADC MTSLLNIDWY RGYTKGMQEV
     MIGYSDSAKD AGVMAAAWAQ YRAQEQLVAV CKKADVKLML FHGRGGSIGR GGGPAHKAIL
     SQPPGSVDGR IRVTEQGEMI RFKFGLPKLA VQSLALYTSA VLEATLLPPP EPKKSWRDCM
     QRIAEESVLH YRGIVREEPD FVEYFRSATP EVELGKLPLG SRPAKRKVDG GIESLRAIPW
     IFAWSQNRLM LPAWLGAGEA LQDAADRGEL ELLREMEEQW PFFETRISML EMVYTKAEPN
     LAKYYELCLV KPELHHLGEK LRQRLQLGIE AVLSLTQATE LMSHTPWSRE SVKLRNPYID
     PLNFLQTELL ARTRREVEPS ADVQLALMLT IAGVAAGMRN TG
//