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Database: UniProt/TrEMBL
Entry: M1TRR3_9CORY
LinkDB: M1TRR3_9CORY
Original site: M1TRR3_9CORY 
ID   M1TRR3_9CORY            Unreviewed;       919 AA.
AC   M1TRR3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=H924_07495 {ECO:0000313|EMBL:AGG66941.1};
OS   Corynebacterium callunae DSM 20147.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG66941.1, ECO:0000313|Proteomes:UP000011760};
RN   [1] {ECO:0000313|EMBL:AGG66941.1, ECO:0000313|Proteomes:UP000011760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG66941.1,
RC   ECO:0000313|Proteomes:UP000011760};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL   Submitted (FEB-2013) 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}.
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DR   EMBL; CP004354; AGG66941.1; -; Genomic_DNA.
DR   RefSeq; WP_015651372.1; NZ_ATVF01000004.1.
DR   AlphaFoldDB; M1TRR3; -.
DR   STRING; 1121353.H924_07495; -.
DR   KEGG; ccn:H924_07495; -.
DR   PATRIC; fig|1121353.3.peg.1528; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011760; 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:AGG66941.1}.
FT   REGION          88..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   919 AA;  103138 MW;  F4A19ABB0028E8A6 CRC64;
     MNDLLRDDIR FLGRILGKVI SEQEGSEVYE LVERARQTSF QIAKGNLEMD TLVEVFKGID
     PEKATPVARA FTHFALLANL AEDLHDAEAR EQALDSGETP PESTLESTWL KLDEAEVKAS
     DVSDVLRNAQ VAPVLTAHPT ETRRRTVFDA QKWITAYMQE RQLLLAAPKN ARTQAKLDAI
     EKNIHRRISV LWQTALIRVA RPRIEDEIEV GLRYYKLSLL EEIPRINRDV VLELRSRYGK
     VIPAKAVIKP GSWIGGDHDG NPYVTADVVA YSTSRAAETV LKYYGRQLHT LEHELSLSDR
     MSSVTEELRE LADAGKNDVP SRVDEPYRRA VHGIRGRILA TTAHLIGEHA VEGTWFKIFE
     PYSSPEEFAA ELKIVDDSLR ASHDELIADD RLAAIYAAVQ SFGFNLYSLD LRQNSESYED
     VLTELFQNAQ VTADYRNLDE AAKTELLLKE LRSPRPLIPN GGWDFTEPTE RELGIFKMAA
     HAVEKFGPNM VPHCIISMAS SVTDVLEPMV LLKEFGLIKA KGDTPVGSID VIPLFETIDD
     LQAGAGILED LWKIDLYRNY LQQRDNVQEV MLGYSDSNKD GGYFSANWAL YDAELQLVDL
     CRSAGVKLRL FHGRGGTVGR GGGPSYDAIL AQPKGAVRGS LRITEQGEII SAKYGSPETA
     RRNLEALVSA TLEASLLDVS DLSDPERAYE IMREISELSL QKYSSLVHED PGFIDYFTQS
     TPLREIGSLN IGSRPSSRKQ TSSVEDLRAI PWVLSWSQSR VMLPGWFGVG TALQQWIGSG
     EQATERIKEL QELNETWPFF TSVLDNMAQV MSKAELRLAK LYSELIPDRE VAQRIYDVIF
     DEYFLTKEMF CVITGSTDLL DENPLLARSV RSRFPYLLPL NVIQVEMMRR YRAGDESKGV
     SRNIQLTMNG LATALRNSG
//
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