ID   Q3B2E8_CHLL3            Unreviewed;       923 AA.
AC   Q3B2E8;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   OrderedLocusNames=Plut_1629 {ECO:0000313|EMBL:ABB24483.1};
OS   Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS   luteolum).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=319225 {ECO:0000313|EMBL:ABB24483.1, ECO:0000313|Proteomes:UP000002709};
RN   [1] {ECO:0000313|Proteomes:UP000002709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 273 / BCRC 81028 / 2530
RC   {ECO:0000313|Proteomes:UP000002709};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelodictyon luteolum DSM 273.";
RL   Submitted (AUG-2005) 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}.
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DR   EMBL; CP000096; ABB24483.1; -; Genomic_DNA.
DR   RefSeq; WP_011358355.1; NC_007512.1.
DR   AlphaFoldDB; Q3B2E8; -.
DR   STRING; 319225.Plut_1629; -.
DR   KEGG; plt:Plut_1629; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_10; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002709; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
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:SF32; PHOSPHOENOLPYRUVATE CARBOXYLASE; 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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ABB24483.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:ABB24483.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002709}.
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   923 AA;  103422 MW;  D9C29592AED65A19 CRC64;
     MISTTSTIID FEKAERDAGF LISCFQEMLC CLGEEALAAR LPRGGRGIDL GHYPDTERAL
     QAYSIFFQLL NMAEENSAAQ NRRTLEAEHG AASLEGLWGR TLLPVQQQGL SEEEARIVLS
     RVQVHPVLTA HPTEAKRKTV LELHRNIYLL LVKRENQMWT PAEQLDIRRE ITSAMETLWR
     TGEILFQKPS IADERANVAH YLENIFPDAI TMMDRRLMKA WEAAGFSARS FKVPDDLPSI
     RFSSWVGGDR DGHPLVTADV TAETLGDMRL KSVGLIDAAL RNLGSKLSLS DRLQDPGEEL
     IGRMDTLRKK HGKRGMDAVR RNEREPWRQF INLMRVSLPP AIRGSGSGSG SAFRYHSARE
     LLGDLAILTR SLEEIGAENI ARELVFPLSR TVQSFGFHLA SLDIRQNSRI HDLALTALIR
     AAGNGEQDET PYIDMSEEKK RELLDRELRS PRPFTRPDMQ AGPEAESVLG CFRVLSGHIR
     SFGTEGIGSL IVSMTRSVSD LLSVYLFARE TGLMTSIKGK SACIVPVVPL FETIGDLEKS
     PGILDAFLSH PVTESSLEYQ RRRDGAKRRV MEVMIGYSDS NKDGGLLTSA WALYRAEEAM
     LEVGRRHNTC IRFFHGRGGS ISRGAGPTHR FIRAQPYGAC NGGMRFTEQG ETIAQKYANR
     ISAVYNLELF MAGVAGSLIR ESRHEKAAHH LEPVMDRLSS ASYSAYRTLI ETEGFVTFFR
     QAAPVDIIEA NRIGSRPSRR TGGDSLDDLR AIPWVFSWNQ ARFSLSGWYG VGSALEALNE
     SDPEAFEDIR IRSHQWPPLR YIISNADTGL AAADLSVMRL YAGLVTEAGL RDKIMGMIED
     EYRKTKRFID ILYSKPLATQ RLNVNRFIEL RREGLGLLHR WQVQRIAEWR KLLDDGRKEE
     ADAMLPELFL TVNAISGGLR TTG
//