ID   C7M9P2_BRAFD            Unreviewed;       942 AA.
AC   C7M9P2;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   04-NOV-2026, entry version 86.
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=Bfae_07300 {ECO:0000313|EMBL:ACU84586.1};
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS   19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Dermabacteraceae; Brachybacterium.
OX   NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU84586.1, ECO:0000313|Proteomes:UP000001919};
RN   [1] {ECO:0000313|EMBL:ACU84586.1, ECO:0000313|Proteomes:UP000001919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC   NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(2009).
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 = phosphoenolpyruvate +
CC         hydrogencarbonate; 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:ARBA00048995, 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; CP001643; ACU84586.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7M9P2; -.
DR   STRING; 446465.Bfae_07300; -.
DR   KEGG; bfa:Bfae_07300; -.
DR   PATRIC; fig|446465.5.peg.719; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; AAAIPQC; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001919; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR   NCBIfam; NF000584; ppc; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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:ACU84586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001919}.
FT   COILED          45..72
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        600
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   942 AA;  105502 MW;  BA1D9AAA902A5D9C CRC64;
     MPHSDAIAVP TLTSEFPVVG DDPHIDAPLR ATVRRLSTLL GGALADQHGQ EMLDLVEQVR
     KLTKEAKSAD SEASAQDVQK RLAELPIEQA TALTRAFSQY FLLANAAEQV YRVRALDERP
     SAESWVPRTV RDIHEEVGTD GLQQAVDSLD VRLVFTAHPT EASRRAVLTK LRRISDILGE
     DTEEGTPERR RQDRDLAELI ETLWQTDELR RQRPTPQDEA RNALYYLREI FRHTMPEMLD
     DLREELRAHG ANLRDDQVPL RFGSWIGGDR DGNPFVTAQV TREVLKLQAE TSIDFAIEVI
     SELILELSVS SELTGEDEEL RASLAEDLQH NSEVDEVQQE LYHEEPYRLK LGAMRSKLNA
     TRERIRTGEA HVHGRDYSDS AELQEDFRVL REALHRHGGE RAADGTLAIA QQVLAASGLN
     LATLDVREHS EKHHDVLSRL FDRVGELDRP YAELSREERT TVLGRELGSR RPLVGSAITE
     DESTLDDATR TTYNVFREIR DAHRLYGTSV IETYIISMTH GADDVLAAAL LAREAGLLSI
     AGSEERRADI GFVPLLEEVS ELRHAGEILD ELLSDPSYRE IVRLRGDRQE VMLGYSDGNK
     DAGVITSQWE IHQAQRSLRD TAARHGVTLR LFHGRGGSVG RGGGPTYDAI LAQPYGVLEG
     EIKFTEQGEV ISDKYMLPSL ARENLDLSLA AVLEGSALHT APRTPAETLE RFGDVMQSVS
     DSSFARYRTL VDDENLPEYF VSATPVEQLG DLNIGSRPSK RTTSEKGLDG LRAIPWVFGW
     TQSRQIVPGW FGAGSGLKAA REAGLEPDLH EMYRSWHFFR TVISNVEMTL AKTDMQIAAH
     YVHSLVPERL WYLFDRIREE YELSVAEIER LTGVLGLLDN QPVLKRTLSV RDRYLDPISY
     MQVAMLQRAR AATARGEELS PELQRALLTT INGVAAGLKN TG
//