ID   G0ASC7_9GAMM            Unreviewed;       889 AA.
AC   G0ASC7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
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};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=Sbal175_0284 {ECO:0000313|EMBL:AEG09580.1};
OS   Shewanella baltica BA175.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG09580.1, ECO:0000313|Proteomes:UP000002249};
RN   [1] {ECO:0000313|EMBL:AEG09580.1, ECO:0000313|Proteomes:UP000002249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA175 {ECO:0000313|EMBL:AEG09580.1,
RC   ECO:0000313|Proteomes:UP000002249};
RX   PubMed=22328742; DOI=10.1128/JB.06468-11;
RA   Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA   Konstantinidis K.T.;
RT   "Genome sequencing of five Shewanella baltica strains recovered from the
RT   oxic-anoxic interface of the Baltic Sea.";
RL   J. Bacteriol. 194:1236-1236(2012).
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; CP002767; AEG09580.1; -; Genomic_DNA.
DR   RefSeq; WP_006083554.1; NC_017571.1.
DR   AlphaFoldDB; G0ASC7; -.
DR   KEGG; sbb:Sbal175_0284; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000002249; 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:AEG09580.1}.
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        553
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   889 AA;  100338 MW;  B50B66F93CD3E1F7 CRC64;
     MVVTKADNMT DMYASLRSNV SMLGQILGDT MRTHLGDSFL EKVEQIRKLA KDSRRGDQAA
     REQMLELLTA LPDEELVPFA KAFNQFLNLA NLSEQFHTIS RNCDELVCVP DPVEQLLGRM
     LNGRVDQTKM LDCLKTLDID LVLTAHPTEI SRRTLIQKYA AIVDCLTEQE NDQLSDRERQ
     QISLRLRQLI AQIWHTNEIR RERPTPVDEA RWGLSTIEES LWHAVPDFLR QLNDQVQKRT
     GQQLPIDIAP VRFSSWMGGD RDGNPFVTAK VTQEVLDRNR HAAARLFLKD IVLLVGELSM
     EEANDELKAY TNNSCEPYRH VLRSIRQRLR DTIDYLNARI EGHNPEVDKS SLIWQESDLK
     APLEMLYKSL TDCGMRLIAN GLLLDILRRL ACFGIHMLRL DIRQDASRHS DVLAELTRYL
     GMGDFNHWDE TEKQAFLLRE LSNRRPLIPS NWQPSADVAE VLNTCRLIAK HPAKALGSYV
     ISMAGKPSDV LTVLLLLKET GCSHPMRVVP LFETLSDLNN AAACITDLLD IDWYRGYTKG
     MQEVMIGYSD SAKDAGVMAA AWAQYHAQEQ LVAVCKQAGV KLTLFHGRGG SIGRGGGPAH
     KAILSQPPGS VDGRIRVTEQ GEMIRFKFGL PKLAVQSLAL YTSAVLEATL LPPPEPKQEW
     RDCMQRIAEE SVGAYRGIVR DEPDFVAYFR AATPEVELGK LPLGSRPAKR RVDGGIESLR
     AIPWIFAWSQ NRLMLPAWLG AGEALQAACE RGEMGLLQEM EREWPFFSTR ISMLEMVYAK
     AEPNLARYYE TCLVPKDLHH LGETLRQRLD LGIKVVLELT KSDSLMAHTP WNRESVKLRN
     PYIDPLNFLQ TELLARTRKE TTETPASEHV QLALMLTIAG VAAGMRNTG
//