ID   C4FAB1_9ACTN            Unreviewed;       941 AA.
AC   C4FAB1;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   13-SEP-2023, entry version 68.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   Name=ppc {ECO:0000313|EMBL:EEP44280.1};
GN   ORFNames=COLINT_03003 {ECO:0000313|EMBL:EEP44280.1};
OS   Collinsella intestinalis DSM 13280.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=521003 {ECO:0000313|EMBL:EEP44280.1, ECO:0000313|Proteomes:UP000003295};
RN   [1] {ECO:0000313|EMBL:EEP44280.1, ECO:0000313|Proteomes:UP000003295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13280 {ECO:0000313|EMBL:EEP44280.1,
RC   ECO:0000313|Proteomes:UP000003295};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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   -!- 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEP44280.1}.
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DR   EMBL; ABXH02000017; EEP44280.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4FAB1; -.
DR   STRING; 521003.COLINT_03003; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000003295; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   InterPro; IPR021135; PEP_COase.
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; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EEP44280.1}; Lyase {ECO:0000313|EMBL:EEP44280.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:EEP44280.1};
KW   Transferase {ECO:0000313|EMBL:EEP44280.1}.
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        605
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   941 AA;  104355 MW;  39F0AEA39F82A630 CRC64;
     MAENTSAEQR LGGFITGDMV TDVMSGTRRI DLTDLAAAVE VLSDIDIPAE LRDNLALFLR
     LERRVLREYD AKVLDVFDEL MMNVIRANAG DPGAEADGEA VDEQGMPASD TPSACAFRDA
     VALIDALPVD QAQVIVRAFT AFFHLANLSE ENYRVAQLRE RERNVSTEDA VDPANALTVA
     FHQLNEEVGG AKATELLSRL EFHPVFTAHP TEARRKAVEG KIRRIARLLE ERPYMGGSDL
     VENERHMLQE IDALVRTSPI ALKKPTPVEE ADTIIDIFDS TLFDTIPVIY RRFDDWVLGE
     VAGTVPPVCP AFFHPGSWIG SDRDGNPNVT AKVSRQVAAK YATHMISKLA DKCRRVGRNL
     TLEAAYTQPS DELLNLWSHQ VEMSEVLTER AREISNSEPH RAVMLVMAAR LDATVARNAD
     TMYRTAEEFL ENLRVVQRSL AAAGARRAAY GPVQTLIWQV ETFGFHMVEM EFRQHSVVHS
     RALADIREHG IHGELAPMTR EVLDTFRAIG SIQKRFGQKM ARRYIISFTK SASHVADVYE
     LANLAFAHAE DVPTLDVIPL FEQLEDLEGC VDVLEEMLAI PAVQNRLAES GRRMEIMLGY
     SDSSKDAGPT TATLALHSAE ERIVAWAEKH DIDLVLMHGR GGAVGRGGGP ANRAVLAQPA
     GSVNCFFKVT EQGEVIFARY GNPALAQRHV ESVAAATLLN SAPSVERTNT EMTARYAEMA
     AALNEASHER YLDLLNTEEF TPWFSCVTPL TEVGLLPIGS RPAKRGLGAK SLDDLRTIPW
     VFSWSQARIN LAAWYGLGTA CEKLGDLELL QRAYREWPLF NTFIDNIEMS IAKTDNRIAK
     MYLALGDRAD LADKVFDEMM LTRSWVLRIV GDAWPLEHRR VLGQAVRVRN PFVDALSLAQ
     VRALREVRAN QDELSEEAKA EFMSLVLETV TGVSAGLQNT G
//