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 24-JAN-2024, entry version 91.
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}.
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DR EMBL; AY517644; AAS01722.1; -; mRNA.
DR AlphaFoldDB; P81831; -.
DR SMR; P81831; -.
DR PaxDb; 3055-EDP01154; -.
DR EnsemblPlants; PNW72303; PNW72303; CHLRE_16g673852v5.
DR Gramene; PNW72303; PNW72303; CHLRE_16g673852v5.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR OrthoDB; 355614at2759; -.
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 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:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 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 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
//
