ID A0A0K1E7D3_CHOCO Unreviewed; 888 AA.
AC A0A0K1E7D3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ECO:0000313|EMBL:AKT36577.1};
GN ORFNames=CMC5_006950 {ECO:0000313|EMBL:AKT36577.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT36577.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT36577.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT36577.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) 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|HAMAP-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; CP012159; AKT36577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1E7D3; -.
DR STRING; 52.CMC5_006950; -.
DR KEGG; ccro:CMC5_006950; -.
DR PATRIC; fig|52.7.peg.742; -.
DR Proteomes; UP000067626; 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; 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 Pyruvate {ECO:0000313|EMBL:AKT36577.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 554
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 888 AA; 96977 MW; DE7169BC28AB3B73 CRC64;
MLGHLLGEVL REQEGQALFD QEERIRLLSI RRRRGPHEGR AQAAAELAEA LATLPAEQVE
PIIRAFTVYF RLVNLAEQHH RIRRARAHAT DAEPQRGSLE ATFLALRRAG VSAQRAREAA
QSLEVTLTVT AHPTEASRRT VLAKLFRLAE YLEQRDRCAL TPVEQERALA AAREEITALW
QTDEIRHERP SVGDEVKNVA WYIEEILWDL LPDVSDQLER AFAHAYNEPL GALPNPVRIH
SWVGGDMDGN PRVTPEVLED AILAYRVRGL RLLVRAAARL GDALSQSSRH VTPPPSLLAS
LDEDARRLPD VAATWAPRTE GEPWRRKLRF VQARLEATLA LGEARRAFLR RRMDGHGSES
PAATPTGNEA AYSAPEELTK DLALVADTLV AAGCARSGAE EVRALLARVR VFGFSIAELE
ARAPAEDARA AARTLSSSTT VEVTSGAARL LGALDAIARA QREGGERACR TLILSMTQGP
DDVLAALACA RAVGLGIKGT AGAHIDIVPL FESHDALNAS ADIVRALLDH PEYREHVKAR
GAQEVMIGYS DSSKEVGLLA AAAALRRTQE ALPEIAREAG IALRIFHGRG ESVARGGGPA
QQAILALPPG AVAGRYKATE QGEALDHKYA RPQLALRTLE LVLGGALLHT LDVQPRPGDA
QHARYAAAFD EMAEGGRRAY RALVWEDPRF ERFFATATPL DAITRLNIGS RPSKRASGGM
ESLRAIPWVF SWTQNRAILP AWYGVGSGLA SFGKKPGGVA QLREMAASWP FFSALLSSVE
MVLAKSEISI FARYAELAPA DVRDAIAPRI LEEHALTRRW IKRILDVSKL LDGNPTLKRS
IALRNPYVDP LSYLQIELLR SERAGADVRD RELLLTLNGI AAGMRNTG
//
