ID A0A0N1G1H8_9ACTN Unreviewed; 914 AA.
AC A0A0N1G1H8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=OK006_5119 {ECO:0000313|EMBL:KPI08995.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI08995.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI08995.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI08995.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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|ARBA:ARBA00001946,
CC 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:KPI08995.1}.
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DR EMBL; LJCU01000218; KPI08995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1G1H8; -.
DR PATRIC; fig|1592326.3.peg.6327; -.
DR Proteomes; UP000037912; 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; 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:KPI08995.1}.
FT ACT_SITE 136
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 568
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 914 AA; 101773 MW; A5253A0942B8E2D6 CRC64;
MSSADDQTTT TSSELRADIR RLGDLLGETL VRQEGPELLE LVEKVRRLTR EDGEAAAELL
RGTELETAAK LVRAFSTYFH LANVTEQVHR GRELRAKRAA EGGLLARTAD RLKDADPEHL
KQTVKNLNVR PVFTAHPTEA ARRSVLNKLR RIAALLETPV IEADRRRYDT RLAENIDLVW
QTDELRVVRP EPADEARNAI YYLDELHAGA VGDVLEDLTA ELERVGVRLP DDTRPLTFGT
WIGGDRDGNP NVTPAVTWDV LILQHEHGIN DALDVIDELR GFLSNSIRYT GATEELLESL
QSDLERLPEI SPRYKRLNAE EPYRLKATCI RQKLENTKQR LATGTPHDEG RDYLGTGELL
RDLTLIQTSL REHRGALFAD GRMNRTIRTL AAFGLQLATM DVREHADAHH HALGQLFDRL
GEESWRYVDM PRDYRAKLLA KELRSRRPLA PTPPPLDAAG EKTLGVFGTV KKALEIFGPE
VIESYIISMC QGADDVFAAA VLAREAGLLD LHAGWAKIGI VPLLETTDEL KAADTILEDM
LSDPSYRRLV ALRGDVQEVM LGYSDSSKFG GITTSQWEIH RAQRRLRDVA HRYGVRLRLF
HGRGGTVGRG GGPSHDAILA QPWGTLEGEI KVTEQGEVIS DKYLVPSLAR ENLELTVAAT
LQASALHTAP RQSDEALARW DAAMDVVSDA AHNAYRRLVE DPDLPAYFFA ATPVDQLADL
HLGSRPSRRP DSGAGLDGLR AIPWVFGWTQ SRQIVPGWFG VGSGLKALRE AGLRQEGDTV
LDEMHEQWHF FQNFLSNVEM TLAKTDLRIA RHYVDTLVPD DLKHVFATIE AEHELTVREV
LRVTGGKELL DTNPVLQQTF SIRDAYLDPI SYLQVALLKR QRDEAAAGAE PDPLLSRALL
LTVNGVAAGL RNTG
//
