ID J9SI53_9ACTN Unreviewed; 955 AA.
AC J9SI53;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=KTR9_2286 {ECO:0000313|EMBL:AFR48923.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48923.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR48923.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR48923.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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}.
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DR EMBL; CP002907; AFR48923.1; -; Genomic_DNA.
DR AlphaFoldDB; J9SI53; -.
DR STRING; 337191.KTR9_2286; -.
DR KEGG; gor:KTR9_2286; -.
DR PATRIC; fig|337191.3.peg.2601; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR Proteomes; UP000003281; 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:AFR48923.1}.
FT ACT_SITE 181
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 617
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 955 AA; 105034 MW; A132242ADA1F1693 CRC64;
MPLPGDAGIL VGMSETVPTR GVPDWRPSIS IVDHIVVDDE GRALTEPLRE DIRLLGGILG
DVVREHSGAD VFDLVEAARV AAFRVRRNEI DRNELADMFV DLDISTAVPV IRAFSHFALM
ANLAEDIHRE RRRAIHVRAG DPPQDSSLAA TYRKLAAAGL GDEEVGRTLA DAAVVPVITA
HPTETRRRTV FEAQNRITEL MRFRGRTELT PDEDAEVTES IRRQILTLWQ TALIRLERLT
IQDEIRSGLR YYDASFFEVV PAINTAVRAA LRATYPDAGL ADEPMIQMGS WIGGDRDGNP
FVNSEVVTLA TTLAAQTAVG HHLSELESLA QELSMSARLI DASDTLFDLA GASADDPGAD
EPFRLALRAI RSRLLATARD MFDDDFLTSS EESLIDGRQP YGHAAELLAD LDVIDDALRA
NNDDSIADDR LLALREAVRT FGFHLSGLDM RQNSDMHEEV VAELLAWAGV HPDYASLEES
ERVRILSAEL SARRPLTSPD AELSELATKE LGIVRAAARA VATFGPAAVP NYIISMCTSV
SDMLEALILL KEAGLYDPDG GTPRCTVRVV PLFETIEDLQ QGAQTLLAVL DVPFYRAMVQ
SQNGIQEIML GYSDSNKDGG YMAANWALYR AELDLVDAAA RSGIRLRLFH GRGGTVGRGG
GPSYDAILAQ PPGAVQGSLR ITEQGEIIAA KYAEPVTARR NLETLLAATI ESSLLDVEGL
GDESDSAYEI MDDIAAKARA AYSRLVHETP GFVEYFTTST PLSEIGALNI GSRPASRKQT
EKISDLRAIP WVLSWTQSRV MLPGWYGTGS AFEEWVGDDP DRLETLRRYY AKWPFFRTVM
SNMAQVLAKS DMGLAHRYAQ LVPDEELRDR VFGMIVDEHE RTIAMCAKIT GTDDLLHDNA
ALKRSVYNRF PYLEPLNLLQ VELLRRFRAG EDTPIVRRGI QLTMNGLATA LRNSG
//