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
//