ID   CAPP2_CHLRE             Reviewed;        1221 AA.
AC   Q6R2V6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 2;
DE            Short=PEP carboxylase 2;
DE            Short=PEPC 2;
DE            Short=PEPCase 2;
DE            EC=4.1.1.31;
GN   Name=Ppc2 {ECO:0000312|EMBL:AAS01721.1};
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).
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:P29194}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AY517643; AAS01721.1; -; mRNA.
DR   AlphaFoldDB; Q6R2V6; -.
DR   SMR; Q6R2V6; -.
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; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Pyruvate.
FT   CHAIN           1..1221
FT                   /note="Phosphoenolpyruvate carboxylase 2"
FT                   /id="PRO_0000166662"
FT   REGION          443..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000250|UniProtKB:P29194"
FT   ACT_SITE        886
FT                   /evidence="ECO:0000250|UniProtKB:P29194"
SQ   SEQUENCE   1221 AA;  131242 MW;  650D1BE414E27273 CRC64;
     MTDSTYDFGA VRDDLTPLED DCKLLGSLLD DCLRVEIGET MFKKIERIRA LAQCASNLSI
     KGDAGASDML SHRLAEELMN LDMDEAVPLT RACGHYLNLS GIAELHHGVR RDRATREPNP
     NSCDAVFARL ITEGVDPEEL YRAVSEQNVE VVLTAHPTQV NRRTLQYKHT RIAALLQQHD
     RSDLTAEERR NMVSELQREV AALWQTDELR RQKPTPLDEA RGGLHIVEQS LWAAVPQYMR
     RLSAALKKHT GHDLPLQATP FRFGSWMGGD RDGNPNVTAK VTAHVTALAR WMAADLYLRE
     IDTLRFELSM NQCSAAVWKM ARRIIAEGHT KRAGVVRAKA AAALHQTATD AASHGGSAAS
     AAAAAAAGGD VVADGTSGGG AAAAAGPAAA AAADDAFTFS RLGRPRPERP STDVRSVGVL
     AGGEGAAFPG GMILGTQPVS AHTAAEVSVP HELPGQDVEG GSEMDFNESR RASDAGDLGA
     SQHPMLGGPS AGASAEPTAH GYTTTATAAA AAADGTQPEP EVPGTPSYAD PGTPDRLGAL
     PGPFTPGPTP FREAANAAMS TAASGGAGGG GGGGANRAAS GLGGDPTFTR RSLMAQRLGT
     SSVQFARAHE HPGFHPYRIV LGHVRDRLAA TRRRMEDLLS GREPAGEAHG GVGAGGGGGG
     GAAPWYESED ELAEPLMACY WSLWECGGGV IADGRLLDLI RRVYTFGMCL MKLDLRQEST
     RHAEALDAVT SYLGLGSYLE WSEDQKIEWL TKELQGRRPL IPADMPMSAE VREVLDTFKV
     AAHLGRDNLG AYVISMTKGA SDVMAVELLQ REARMQVGAE AGGRGGGGPE DGGSLRVVPL
     FETLEDLDAA EDVMTRLLTN PWYREHLRAV HGDAQEVMLG YSDSGKDAGR LAANWALYKC
     QERLVAITKA NNVKLTLFHG RGGTVGRGGG PTHIAIQSQP PGSVEGTFRI TEQGEMVQAK
     FGISGVALSQ LETYTTAVLL ATMRPPSPPR REEWRAVMEM LSRVSCESYR NIVHHSPLFL
     RYFKHATPEA ELGNLYIGSR PARRRNKDAS ISTLRAIPWI FAWTQNRLIL PSWLGIGAAL
     TAAMTQGHLP TLQAMYREWP FFGSTVDLIE MILAKTDPRI AALYEEVLVN DPEEKKLGAE
     LRERLQRCQG AILKVTGHEN LLSNNPTLSK LISMRSPFVD PINILQVEVL RRLRQDPNNM
     RLRDALLISI NGIAAGMRNT G