ID   D2S8W2_GEOOG            Unreviewed;       939 AA.
AC   D2S8W2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, 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=Gobs_0841 {ECO:0000313|EMBL:ADB73605.1};
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB73605.1, ECO:0000313|Proteomes:UP000001382};
RN   [1] {ECO:0000313|EMBL:ADB73605.1, ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX   PubMed=21304698;
RA   Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA   Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT   20).";
RL   Stand. Genomic Sci. 2:158-167(2010).
RN   [2] {ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
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   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) 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,
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}.
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DR   EMBL; CP001867; ADB73605.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2S8W2; -.
DR   STRING; 526225.Gobs_0841; -.
DR   KEGG; gob:Gobs_0841; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000001382; 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   Pyruvate {ECO:0000313|EMBL:ADB73605.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001382}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   939 AA;  102921 MW;  0E2065F941A03AD0 CRC64;
     MSEATVDVAD LRHHGGAEED GADAADAPLR EDIRLLGRVL GEVIREQSGD DVLALVEATR
     VEAFRLRRSE VDRADVAARL DGLDVRSANH VIRAFSHFSL LANLAEDVHH ERRRRFHRLE
     GSPPQKGSLA ATFELLDAAH LDADVVAREL AGALVSPVVT AHPTEVRRRT ISRVQRQVTE
     LIRRRDRSAP GEADDPAWSG ELQRAVLTLW QTALLRLSRL RLADEIDEAL RYYEMSLFEV
     VPAINAELRR ALHARWPSAG SDRPVLRPGS WIGGDRDGNP FVTADAVHLA STRQAQTALG
     HHLSELLALH DELSMSDRLI TPTPELAQLA AASGDDSRFR ADEPYRRALY GVHARLAATA
     QRVLGSVPGP PPHAVLEPYA TPEEVLADLA TVDASLRAHG AAALADDRLA RLREAVEVFG
     FHLAGLDMRQ NSAVHAEVLA ELFAWAGVCP DYAALDEKQR VELLVGELRM RRPLVRPDAA
     LSDLARGELD VLLAAADQVR ALGPEAVPNY VISMCESVSD VLEVAVLLKE VGLLDPGGDG
     GPTCPVGISP LFETIGDLQH AAETLTAVLG QPLYRALLRN RGDVQEVMLG YSDSNKDGGY
     LAANWALYRA ELALVEVARR EGVRLRLFHG RGGTVGRGGG PSYDAIRAQP PGAVAGALRI
     TEQGEVIAAK YAEPDRARRN LEAMVAATLE ASLLDTEGLG DDAEPAYALL DDLAARAQQA
     YRALVHETPG FVEWFRAATP IGELAELNIG SRPPSRKAGD SIADLRAIPW VFSWSQARIM
     LPGWYGTGSA LESWVEGDPA RLTRLQELHR RWPWFRTMLS NMGMVLAKTD LDLAARYAEL
     VPDEQLRHRV FDQLTAEHER SCRMLLAVTG DDRLLADNPA LARSIRNRFP YLEPLHHLQV
     EMLRRRRGHD GQDGDDDELV RRNIQLTING IATALRNSG
//