ID M1L664_9PROT Unreviewed; 937 AA.
AC M1L664;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 03-MAY-2023, entry version 53.
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=CONE_0289 {ECO:0000313|EMBL:AGF48103.1};
OS Candidatus Kinetoplastibacterium oncopeltii TCC290E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208920 {ECO:0000313|EMBL:AGF48103.1, ECO:0000313|Proteomes:UP000011541};
RN [1] {ECO:0000313|EMBL:AGF48103.1, ECO:0000313|Proteomes:UP000011541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC290E {ECO:0000313|EMBL:AGF48103.1,
RC ECO:0000313|Proteomes:UP000011541};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003805; AGF48103.1; -; Genomic_DNA.
DR RefSeq; WP_015396791.1; NC_020299.1.
DR AlphaFoldDB; M1L664; -.
DR STRING; 1208920.CONE_0289; -.
DR KEGG; kon:CONE_0289; -.
DR PATRIC; fig|1208920.3.peg.74; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000011541; 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:AGF48103.1}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 582
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 937 AA; 107424 MW; 5A58497ECB018C85 CRC64;
MQISPLRQEI RLLGKMLGEI IYSCEGKRLF DIIELIRRSA IRLRKNKKDH DNESLEEYIS
KLEGNDPNTV ARAFSYFMHL VNIAEDNDQN RRHKEHLSEL DYPIRGSLKD VIKKLNSNGV
NSCAINELLN ESCIVPVLTA HPTEIQRKST LDAHRNISRK LIERNSEKDK ENLKEIDLEL
LGYIAIMWQT RILRYSSLTV NDEIENALSY YRSTFLSTIP KLYRDLSNLL NNSKNSTSLP
LKPFLRMGSW IGGDRDGNPS VDELTLEQAM IRQSSVIFEH YLKEVFALKT ELSVSNLLVD
VDKEILSLAE ESKDLSPHLK DEPYRKALVG IYARLAVTSE KLTGKNLARR AILNALPYKV
SEEFYNDLNT ISSSLEKHHG NLINSLRLKN LQQSVKVFGF HLTTLDLRQN SDVHEKILDE
LFAQANIILD DKKNKYSDLN EEDKIKILRF ELMQGRQLVS PWFEYSAETT KELKIFRTAA
RIRSEYGKDS IKQYIVSHTE TLSDLLEVLV IQKETGLIKP AYYPQIENEG LMVVPLFETI
TDLQNSAEIM SRWINLPEVR SIISDSNHNI QEVMLGYSDS NKDGGFLTSN WELYQAERNL
VEVFRSNNIK LRLFHGRGGS VGRGGGPSFE AILAQPPGAV SGQIRLTEQG EVVHGKYNNA
EVGKWHLELI VAATLESSLY VTTNKKNMDN IYVDKYGEAM SFMSRHAEKI YRNLIYEKPG
FTEYFFTSTP INEIAELNIG SRPSSRKNLQ NIEDLRAIPW SFSWSQCRLM LTSWYGVGSA
IENFLDNGAS VIAKSKNDRL SLLRVMIREW PIFKTLISNM EMVLIKSDLG IASCYSKLVP
NQTLRNNVFN AISLEYYKTI EMLRLLTNRD LLEDNPTLLN ALKERFTYID PLNYLQVELL
RRHRYGYNSL SQSSKDMTKR DIHITINGIA AGLRNSG
//
