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Database: UniProt/TrEMBL
Entry: J9SI53_9ACTN
LinkDB: J9SI53_9ACTN
Original site: J9SI53_9ACTN 
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
//
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