ID   A9WHN1_CHLAA            Unreviewed;       939 AA.
AC   A9WHN1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Caur_3161 {ECO:0000313|EMBL:ABY36357.1};
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36357.1, ECO:0000313|Proteomes:UP000002008};
RN   [1] {ECO:0000313|Proteomes:UP000002008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC   {ECO:0000313|Proteomes:UP000002008};
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
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         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP000909; ABY36357.1; -; Genomic_DNA.
DR   RefSeq; WP_012259010.1; NC_010175.1.
DR   RefSeq; YP_001636746.1; NC_010175.1.
DR   AlphaFoldDB; A9WHN1; -.
DR   STRING; 324602.Caur_3161; -.
DR   EnsemblBacteria; ABY36357; ABY36357; Caur_3161.
DR   KEGG; cau:Caur_3161; -.
DR   PATRIC; fig|324602.8.peg.3568; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   InParanoid; A9WHN1; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; 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.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002008}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   939 AA;  106180 MW;  B9F9B80275D525EF CRC64;
     MSGRTTANEH DLLSANIRAL GDALGRVIIG QHGSEALALV EQVRRMAKDL RNAPTNTDPQ
     ALPQLIADLD LPQLRSLVKA FTLYFGLVNL AEGVERLRVL RARDLRHAPA PRAESIADAI
     ELLKRHGVPA PAIQEWLDHA LIMPVLTAHP TESRRRTILI KLRRIFDTLV DLTFGERLVL
     PADRQAALTR IEREIVGLWQ SDDVRNRRPS VLDEVENGLF FFQTVLWELL PHIYREMSDA
     LQAAYPDHPW RLPPFLRFGS WMGGDRDGNP FVTPEVTVET VRLMRSAMLR YLIDCLDRLI
     TDLSQSVQQV KVDTAIIDRI AEYRELMPDA AATLNPHYRC EPYRQLCHFI QARLHNTLQY
     TLDYTPRWGI DPPLARRPDI YYHSRELLAD LDLIDASLRN NGSTLIAEGL LRDVRTLVAV
     CHLHTATLDV RQHASRHTAA LSEILAAAGV VDDYEALDEA ERIAVLSVEI RRPRPLTPSR
     LSHFSPATAE TIHTFRVIAA ISEQLDPEIF QTYIISTTSQ VSDLLAVLLL CRDAGLYQPG
     QASQLHIVPL FETGDDLQRA PALLDELLRL PVYREHLALR DNLQEVMLGY SDSNKEGGFV
     AANWALYRAQ VELTAVTDRH GVRLRLFHGR GGAVGRGGAV GRGGGPAGQA ILAQPPGTLH
     GQIKVTDQGE MISDRYLDPR TAHRHLEQVV NAVLRAGFPG MARQPEPTWL AAMEEMATTA
     RTVYRQLVYE DPDFLIYFRS ATPVAEFNRL RIGSRPVSRR KSDRIEDLRA IPWVFSWMQS
     RHTIPGWFGL GSALEAFVEA DPHHLHLLRT MYQHWPFFST LLDNAQMIML KADMNIARAY
     ASLVPDRHLA ERIFQRIESE FRRTERMICQ ITERNDLLAH QPVLQRAIRQ RNPYIDPLSF
     VQIELLRRLR AAPPEEQGEL ETVLLMSING IAAGLKNTG
//