ID   D0LCT8_GORB4            Unreviewed;       945 AA.
AC   D0LCT8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Gbro_2367 {ECO:0000313|EMBL:ACY21609.1};
OS   Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS   / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY21609.1, ECO:0000313|Proteomes:UP000001219};
RN   [1] {ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACY21609.1, ECO:0000313|Proteomes:UP000001219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC   NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RX   PubMed=21304674;
RA   Ivanova N., Sikorski J., Jando M., Lapidus A., Nolan M., Lucas S.,
RA   Del Rio T.G., Tice H., Copeland A., Cheng J.F., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Han C., Detter J.C., Brettin T., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Gordonia bronchialis type strain (3410).";
RL   Stand. Genomic Sci. 2:19-28(2010).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001802; ACY21609.1; -; Genomic_DNA.
DR   RefSeq; WP_012834164.1; NC_013441.1.
DR   AlphaFoldDB; D0LCT8; -.
DR   STRING; 526226.Gbro_2367; -.
DR   KEGG; gbr:Gbro_2367; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001219; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
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; 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; 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   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:UP000001219}.
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        607
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   945 AA;  104194 MW;  E94F28109F5A0BBC CRC64;
     MSQSVPSRGA PAWRPSISIV DHITVDDEGR ALTEPLREDI RLLGGLLGDV IREHSGDEVF
     ELVEAARVAA FRIRRNEIDR GELADMFSGV SLDVVMPVIR AFSNFALLAN LAEDIHRERR
     RAIHLRAGDP PQDSSLAATY TKLAEAGLDD EQVGRALADA TVVPVITAHP TETRRRSVFE
     AQNRITELMR YRSRSELTPA EDDVVIKAIR RQILTLWQTA LIRLERLTIQ DEIRSGLRYY
     DASFFDVVPK INTSVRASLR AAYPDAGLAD DPMIRMGSWI GGDRDGNPFV TDEIVEMATT
     LAARTAIGHH LSELHKLAEE LSMSTRLMDP GEALYELAGV PADDPKADEP FRLALRHIRS
     RLATTATEMF GEEVMKAADL FLVNGKPAYA DAAELLADLD VIDAALRHGK DDILADDRLL
     TLRESVRTFG FNLSGLDMRQ NSDMHEEVIA ELLAWAGVHP DYASLDEDER VAILSEELQK
     RRPLTRPDAD LSELAVKELG IVRAAARAVA TFGPQAVPNY IISMCTSVSD MLEPMILLKE
     AGLIDIDAES GTLTSTVRIV PLFETIEDLQ QGATTLLAAL DLPFYRGLVD SQAGMQEIML
     GYSDSNKDGG YMAANWALYR GELDLVEAAA KAGIRLRLFH GRGGTVGRGG GPSYDAILAQ
     PPGAVQGSLR ITEQGEIIAA KYAEPVSAER NLETLLAATI ESSLLDVEGL GDDSEDAYAI
     MDELAALARS AYSKLVHDTP GFVEYFTTST PLSEIGALNI GSRPASRKQT EKISDLRAIP
     WVLSWTQSRA MLPGWYGTGS AFAEWIGDSD DRLATLQRYY TEWPFFRSVM SNMAQVLAKS
     DMNLAHRYAQ LVPDEELRDK VFGMIVGEHE RTIAMYSKIT GTDDLLADNA ALKRSVYNRF
     PYLEPLNLLQ VELLRRFRAG DDEPRIRRGI QLTMNGLATA LRNSG
//