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CAPP_MYCS2
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   25-MAY-2022, entry version 97.
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; Actinobacteria; Corynebacteriales; 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}.
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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.MSMEI_3019; -.
DR   EnsemblBacteria; ABK70062; ABK70062; MSMEG_3097.
DR   EnsemblBacteria; AFP39483; AFP39483; 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   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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
 
 
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