ID A0A2A9F2N6_9MICO Unreviewed; 907 AA.
AC A0A2A9F2N6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=ATJ88_3451 {ECO:0000313|EMBL:PFG44715.1};
OS Isoptericola jiangsuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=548579 {ECO:0000313|EMBL:PFG44715.1, ECO:0000313|Proteomes:UP000224130};
RN [1] {ECO:0000313|EMBL:PFG44715.1, ECO:0000313|Proteomes:UP000224130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21863 {ECO:0000313|EMBL:PFG44715.1,
RC ECO:0000313|Proteomes:UP000224130};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFG44715.1}.
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DR EMBL; PDJJ01000001; PFG44715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9F2N6; -.
DR Proteomes; UP000224130; Unassembled WGS sequence.
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; 2.
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:PFG44715.1}.
FT ACT_SITE 163
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 561
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 907 AA; 99631 MW; 62362A58AE188554 CRC64;
MTDNNGQHSP STGAIERVVA RHEMPDPLRE DIRLLGGLLG SVLRESGGQD LLDDVEHLRE
LTIRAYGVED GGVALAEAAD VVAGFSLERA EQVARAFTCY FHLANLAEEY HRVRVLRQRE
SEAGAAIEES LPAAFTQLAE EVGRDEALRR LGELEFRPVL TAHPTEARRR AVSGAVRRVS
SLLAERDTMH LGGTSRTENE RRLLAEIDTM WRTSPIRANK PTVLDEVKTA MGVFDATLFE
TFPEVYRRLD DWLLDDEAGR RAPLAKPFVF LGSWIGGDRD GNPNVTAEVT RQAATLAAEH
ALTALENATR ATGRKLTLEE ASTPASGELR ALWQKMRQLS DELAAQAASE SPNEPHRAAV
LAIAGRVRAT RTRDADLAYT NPEELEADLR VVQRSLIDAG APRAAYGDLQ RLVWQVETFG
FHLAEIEVRQ HSQVHAAALA EIEEKGVHGD LSDRTREVLD TYRALGAVQK RFGVRAARRY
IVSFTQAPEH LAAVYQLAEL AFEGSDDVPV VDAVPLFETF ADLENSVEIL EAMLEMPQVQ
RRLAENGRRV EVMLGYSDSS KDVGPVAATL ALHSAQSRIA QWAARHDITL TQFHGRGGAL
GRGGGPANRA VLAQPPHSVD GRFKLTEQGE VILARYGDPT IAARHIEQVA AATLLASAPS
TEKRNATTAE RFAPLAASLD ATSRARFHAL VKSEGFPQWF AQVTPLEEVG LLPIGSRPAK
RGLSVNSLDD LRAIPWVFSW SQARINLAGW FGLGTALREF GDLDVLRAAY TEWPLFATLL
DNIEMSLAKT DERIAEQYLA LGDRDDLAQM VLDELRLTRE WVLKITGNGW PLASRRVLGR
AVQLRSPYVD ALSLLQVRAL RALRTQGVSE GLTVADGEWV DGGYKDRWQH LLLLTVNGVS
AGLQNTG
//
