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,
CC ECO:0000256|HAMAP-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
//
