ID CAPP_MYCS2 Reviewed; 933 AA.
AC A0QWX4; I7FL87;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN OrderedLocusNames=MSMEG_3097, MSMEI_3019;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND IDENTIFICATION OF N-TERMINUS.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK70062.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39483.1; -; Genomic_DNA.
DR RefSeq; WP_011728811.1; NZ_SIJM01000002.1.
DR RefSeq; YP_887412.1; NC_008596.1.
DR AlphaFoldDB; A0QWX4; -.
DR SMR; A0QWX4; -.
DR STRING; 246196.MSMEG_3097; -.
DR PaxDb; 246196-MSMEI_3019; -.
DR GeneID; 66734500; -.
DR KEGG; msg:MSMEI_3019; -.
DR KEGG; msm:MSMEG_3097; -.
DR PATRIC; fig|246196.19.peg.3058; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT CHAIN 1..933
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025566"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 593
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 933 AA; 103351 MW; 33F2EAC46B98F7D8 CRC64;
MADSNDTALE PFGSVQRTHI GREASEPMRE DIRLLGAILG DTVREQNGEE VFDLVERARV
ESFRVRRSEI DRSELADMFS GVDAHQAIPV IRAFTHFALL ANVAEDIHRE RRRAVHVAAG
KPPQDSSLAA TYRKLDAADL DVDKVADTLT GALVSPVITA HPTETRRRTV FDTQHRITEL
MRLRLHGHTR TDDNRDIETE LRRHILTLWQ TALIRLSRLK ISDEIETGLR YYEAAFFDVI
PQVNAEVRDA LRKRWPDAKL LEEPILRPGS WIGGDRDGNP NVTPEVVRHA TGRAAYVALA
HYFEQITALE QELSMSARLV KVTPALAALA DACHEPARAD EPYRRALRVI HARLTSTARE
ILDEQPEHGL DLGLPRYQTP AEFLADLDAV DGSLRANGSR VLADDRLGRL REAVRVFGFH
LSGLDMRQNS DVHEEVVAEL LAWAGVHPDY TSLSEPQRVE LLAAEIATRR PLIREGAELS
ELAQKELGIV AAAARAVKVF GPQAVPNYII SMCQSVSDML EAAVLLKEAG LLDISGSTPY
APVGVVPLFE TIDDLQRGSS ILEAALDLPE YRTMVDARDG HQEVMLGYSD SNKDGGYLAA
NWALYRAELD LVESARKTGI RLRLFHGRGG TVGRGGGPSY DAILAQPPGA VKGSLRITEQ
GEVIAAKYAE PRIAHRNLET LLAATLEASL LDVEGLGEEA EPAYQVLDEL AALAQRAYSE
LVHETPGFVE YFKTSTPVSE IGALNIGSRP TSRKPTTSIA DLRAIPWVLA WSQSRVMLPG
WYGTGSAFEN WIGTDPDGAR LRVLQDLYAR WPFFRTVLSN MAQVLAKADM GLAARYSELV
EDADLRARVF DKIVAEHDRT IRMHRLITGQ DDLLADNAAL ARSVFNRFPY LEPLNHLQVE
LLRRYRSGET DELVQRGILL TMSGLATALR NSG
//
