ID A0A076NM46_9CORY Unreviewed; 882 AA.
AC A0A076NM46;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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_1 {ECO:0000313|EMBL:SNV59732.1};
GN Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN ORFNames=CIMIT_02405 {ECO:0000313|EMBL:AIJ32910.1}, SAMEA4535761_00546
GN {ECO:0000313|EMBL:SNV59732.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ32910.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ32910.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ32910.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SNV59732.1, ECO:0000313|Proteomes:UP000215374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13015 {ECO:0000313|EMBL:SNV59732.1,
RC ECO:0000313|Proteomes:UP000215374};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; CP009211; AIJ32910.1; -; Genomic_DNA.
DR EMBL; LT906467; SNV59732.1; -; Genomic_DNA.
DR RefSeq; WP_038588629.1; NZ_LT906467.1.
DR AlphaFoldDB; A0A076NM46; -.
DR STRING; 156978.CIMIT_02405; -.
DR KEGG; cii:CIMIT_02405; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000028780; Chromosome.
DR Proteomes; UP000215374; Chromosome 1.
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:AIJ32910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028780}.
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 546
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 882 AA; 98016 MW; 8BC6CD4EBFC9D74E CRC64;
MSVQPADHVR EDIRLLGRVL GRVLAEQEGQ EIFDLVESTR RTAFDIAHGD AAPEDLLAVF
RDMDITKMNL VARAFSHFAL LTNLVEDLDD EKAAAPVSLR TSFAHLKDSG VDADKVAELI
AGAQVSPVLT AHPTETRRRT VFDTQTHIKR LLSELHAGAD PAAIEREMEL RMTLLWQTAL
IRIARPRLED EIDVGLRYYK LSLLEQIPAL NRAIRYELRD TFDRDLALTP VMRPGSWIGG
DHDGNPYVNA ETLTYATRQA ADTVLNHYLD ELGELERELS LSDRYSTCSA ELSQLADVAN
NTAESRVDEP YRRAIYGIRH RVAATRDVLA GSASAGTPYA DPGELLADLD VIDASLRAHG
GAIIANDRLN RLRSAVTTFG FHLYTLDLRQ NSESFEKVVA EVLSVAGVCE NYAALAEEDR
VEVLVDELRT PRPLLRAEAQ LSDDTRKEMG ILTAAARAVR DLGQGAIAQC IIAMTGTVSD
ILEPMVLLKE VGLGSVNVVP LFETIEDLAH GARILEDLWS LPFYREHLRA RGDVQEVMLG
YSDSNKDGGY LQANWALYDA ELALVELCNR HGIRLRLAHG RGGAVGRGGG PTYDAILAQP
KGAVDGSIRI TEQGEIISAK YGSPETARRH LEAFVAGTLE ASLLDTEPIA DPTRAYDIMR
TLAAYSGEKY NELIGDPGFI DYFTQSTPLH EIGELNLGSR PASRKQTTAI SDLRAIPWVL
SWAQSRTNVP GWFGVGTAVE RWAGESEERW DDLRELYRDW PFFRSVLSNM AQVMAKAELS
LARLYADLVE DREVAERIYT LIAEEFERTK QVYFRITGHA DLVAENQRQA RSLKRRYPYL
LPLNAVQLEL LRRYRAGDET FLVSKTIQVT MNGLATALRN AG
//
