ID   CAPP4_ARATH             Reviewed;        1032 AA.
AC   Q8GVE8; Q9CA39; Q9SX35;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 4;
DE            Short=AtPPC4;
DE            Short=PEPC 4;
DE            Short=PEPCase 4;
DE            EC=4.1.1.31;
GN   Name=PPC4; OrderedLocusNames=At1g68750; ORFNames=F14K14.14, F24J5.1;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12805623; DOI=10.1104/pp.102.019653;
RA   Sanchez R., Cejudo F.J.;
RT   "Identification and expression analysis of a gene encoding a bacterial-type
RT   phosphoenolpyruvate carboxylase from Arabidopsis and rice.";
RL   Plant Physiol. 132:949-957(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle.
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in flowers and siliques,
CC       and detectable in roots. {ECO:0000269|PubMed:12805623}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD49968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ532903; CAD58727.1; -; mRNA.
DR   EMBL; AC008075; AAD49968.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011914; AAG52040.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34835.1; -; Genomic_DNA.
DR   PIR; C96712; C96712.
DR   RefSeq; NP_177043.2; NM_105548.5.
DR   AlphaFoldDB; Q8GVE8; -.
DR   SMR; Q8GVE8; -.
DR   BioGRID; 28427; 6.
DR   STRING; 3702.Q8GVE8; -.
DR   iPTMnet; Q8GVE8; -.
DR   PaxDb; 3702-AT1G68750-1; -.
DR   ProteomicsDB; 240315; -.
DR   EnsemblPlants; AT1G68750.1; AT1G68750.1; AT1G68750.
DR   GeneID; 843206; -.
DR   Gramene; AT1G68750.1; AT1G68750.1; AT1G68750.
DR   KEGG; ath:AT1G68750; -.
DR   Araport; AT1G68750; -.
DR   TAIR; AT1G68750; PPC4.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   InParanoid; Q8GVE8; -.
DR   OMA; TKHYDEQ; -.
DR   OrthoDB; 355614at2759; -.
DR   PhylomeDB; Q8GVE8; -.
DR   BioCyc; ARA:AT1G68750-MONOMER; -.
DR   BRENDA; 4.1.1.31; 399.
DR   PRO; PR:Q8GVE8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8GVE8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; ISS:TAIR.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:TAIR.
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; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
DR   Genevisible; Q8GVE8; AT.
PE   2: Evidence at transcript level;
KW   Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium; Photosynthesis;
KW   Reference proteome.
FT   CHAIN           1..1032
FT                   /note="Phosphoenolpyruvate carboxylase 4"
FT                   /id="PRO_0000166660"
FT   REGION          377..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1032 AA;  116586 MW;  750116B15B9ECA3E CRC64;
     MTDTTDDIAE EISFQSFEDD CKLLGSLFHD VLQREVGNPF MEKVERIRIL AQSALNLRMA
     GIEDTANLLE KQLTSEISKM PLEEALTLAR TFTHSLNLMG IADTHHRMHK VHNVTQLARS
     CDDIFSQLLQ SGISPDELYK TVCKQEVEIV LTAHPTQINR RTLQYKHIRI AHLLEYNTRS
     DLSVEDRETL IEDLVREITS LWQTDELRRQ KPTPVDEARA GLNIVEQSLW KAVPQYLRRV
     SNSLKKFTGK PLPLTCTPMK FGSWMGGDRD GNPNVTAKVT KEVSLLSRWM AIDLYIREVD
     SLRFELSTDR CSDRFSRLAD KILEKDYDRG KSNFQKQQSS SCLPTQLPAR AHLPACIDFG
     ESRHTKFEIA TTDYMPPNLQ KQNEQDFSES DWEKIDNGSR SGLTSRGSFS STSQLLLQRK
     LFEESQVGKT SFQKLLEPPP LKRAGSAPYR IVLGEVKEKL VKTRRLLELL IEGLPCEYDP
     KNSYETSDQL LEPLLLCYES LQSSGARVLA DGRLADLIRR VSTFGMVLVK LDLRQEAARH
     SEALDAITTY LDMGTYSEWD EEKKLEFLTR ELKGKRPLVP QCIKVGPDVK EVLDTFRVAA
     ELGSESLGAY VISMASNASD VLAVELLQKD ARLALTSEHG KPCPGGTLRV VPLFETVNDL
     RAAGPSIRKL LSIDWYREHI QKNHNGHQEV MVGYSDSGKD AGRFTAAWEL YKAQENVVAA
     CNEFGIKITL FHGRGGSIGR GGGPTYLAIQ SQPPGSVMGS LRSTEQGEMV QAKFGIPQTA
     VRQLEVYTTA VLLATLKPPQ PPREEKWRNL MEEISGISCQ HYRSTVYENP EFLSYFHEAT
     PQAELGFLNI GSRPTRRKSS SGIGHLRAIP WVFAWTQTRF VLPAWLGVGA GLKGVSEKGH
     ADDLKEMYKE WPFFQSTLEL IEMVLAKADI PMTKHYDEQL VSEKRRGLGT ELRKELMTTE
     KYVLVISGHE KLLQDNKSLK KLIDSRLPYL NAMNMLQVEI LKRLRRDEDN NKLRDALLIT
     INGIAAGMRN TG
//