ID   CAPP1_CHLRE             Reviewed;         974 AA.
AC   P81831; Q6R2V5;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE            Short=PEP carboxylase 1;
DE            Short=PEPC 1;
DE            Short=PEPCase 1;
DE            EC=4.1.1.31;
GN   Name=Ppc1 {ECO:0000312|EMBL:AAS01722.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=137c / CC-125;
RX   PubMed=15941397; DOI=10.1111/j.1365-313x.2005.02416.x;
RA   Mamedov T.G., Moellering E.R., Chollet R.;
RT   "Identification and expression analysis of two inorganic C- and N-
RT   responsive genes encoding novel and distinct molecular forms of eukaryotic
RT   phosphoenolpyruvate carboxylase in the green microalga Chlamydomonas
RT   reinhardtii.";
RL   Plant J. 42:832-843(2005).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 16-30, ACTIVITY REGULATION, AND SUBUNIT.
RC   STRAIN=cw15 {ECO:0000269|PubMed:9512480};
RX   PubMed=9512480; DOI=10.1042/bj3310201;
RA   Rivoal J., Plaxton W.C., Turpin D.H.;
RT   "Purification and characterization of high- and low-molecular-mass isoforms
RT   of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtii. Kinetic,
RT   structural and immunological evidence that the green algal enzyme is
RT   distinct from the prokaryotic and higher plant enzymes.";
RL   Biochem. J. 331:201-209(1998).
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle. {ECO:0000250|UniProtKB:Q02909}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by glutamine and dihydroxyacetone
CC       phosphate. Inhibited by glutamate, aspartate, 2-oxoglutarate and
CC       malate. {ECO:0000269|PubMed:9512480}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.1.;
CC   -!- SUBUNIT: Exists as a homotetramer or heterooligomer.
CC       {ECO:0000269|PubMed:9512480, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY517644; AAS01722.1; -; mRNA.
DR   AlphaFoldDB; P81831; -.
DR   SMR; P81831; -.
DR   STRING; 3055.EDP01154; -.
DR   EnsemblPlants; PNW72303; PNW72303; CHLRE_16g673852v5.
DR   Gramene; PNW72303; PNW72303; CHLRE_16g673852v5.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   BRENDA; 4.1.1.31; 1318.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm;
KW   Direct protein sequencing; Lyase; Magnesium; Pyruvate.
FT   CHAIN           1..974
FT                   /note="Phosphoenolpyruvate carboxylase 1"
FT                   /id="PRO_0000166661"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250|UniProtKB:Q02909"
FT   ACT_SITE        604
FT                   /evidence="ECO:0000250|UniProtKB:Q02909"
FT   CONFLICT        28..30
FT                   /note="GLR -> DLL (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   974 AA;  108907 MW;  BD9501207F970196 CRC64;
     MQLSATSGRT SFRVSQDLRT GPANFLSGLR DDDSLLRQVF FSILRHHHPN LAAKVDVIYA
     LSQAWCTSQS DNDFELMVKY VSDLKPEERI LVASSFSHML NLHNLTEEVN SSQIGRAVRL
     GEMDSPTRDT NHSLLKLTTT NGFTPQQVYD TLCSQTVELV LTAHPTQALR ASLLKKYAIV
     RRELDTLHSK RMSEYEKIET LEAIRAAVQA AWRTDEIRRS KPTPQDEMRS GLSYFSTVIF
     DVVPVFHRRV DTALEKLGLP RLPLDRALFK FGSWMGGDRD GNPNVTAETT RDVVVLARLE
     AVNVYFRQVE GLMFDLSIWR CSPEMKELAE RLAAAESRDA ARVAEERKRR NYVDFWAPIP
     PTEPFRVVLA HMRDRLYNTR QVLHQCLIHT HMSVRGALEE AGAYVDIEDM ARPLKLMYDS
     LMSTGDESVA NARLLDLLRQ IRTFGLCMMG LDVRQESTRH TEVMDAVTTY LGLGSYASWD
     EPKRLAFLLG ELQGKRPLMP PGMDMSPEVK EVVRTLRILS ELPGDSLGAY IISMAKTASD
     VLAVVLLQRE TGVRPALRVV PLFETLDDLH NAPGTMTTLL GNDWYRGHIN GVQECMIGYS
     DSGKDAGRLA AAWALYETQE KLVEVAAGCG VRLVLFHGRG GTVGRGGGPT HMAIRSQPSG
     TINGHLRVTV QGEIIEQQFG EKEVCFRTLD LYTSAVLEAA LDPPPAPAQE WRDLMSLLAT
     ESCDMYRSVV YRTPEFYDYF MQSTAASELG RLNIGSRPSS RKSGGIETLR AIPWIFAWTQ
     QRLHLPVWLG IGEALEAAID KGYGPVLQDM YANWPFFTST LDLVEMVLAK ADSRLSAFYE
     RTLVDSSLAP LGQRLRELLA KTQQNILIVV RKSVLLEGNT PSQMSTPNLD EKIRLRSPYV
     APLNVLQALS LQGLRKFRDG GDTEYNPSDP EIIDLLSRDP HKKGEGAQHP FVSAMDDCLM
     ITIKGIAAGM QNTG