ID   L0IXX6_9MYCO            Unreviewed;       931 AA.
AC   L0IXX6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=Mycsm_02866 {ECO:0000313|EMBL:AGB23192.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB23192.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA   Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) 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, ECO:0000256|HAMAP-
CC         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}.
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; CP003078; AGB23192.1; -; Genomic_DNA.
DR   RefSeq; WP_015306771.1; NC_019966.1.
DR   AlphaFoldDB; L0IXX6; -.
DR   STRING; 212767.Mycsm_02866; -.
DR   KEGG; msa:Mycsm_02866; -.
DR   PATRIC; fig|710686.3.peg.2892; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010844; 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:AGB23192.1}.
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   931 AA;  103045 MW;  46ADB222FDF7717E CRC64;
     MAEGPDVALA PIGSVRRTQV GREATEPMRE DIRLLGTILG DTVREQNGEE VFDLVERARV
     ESFRVRRSEI DRAELARMFD GIDIHQAIPV IRAFSHFALL ANVAEDIHRE RRRAVHVAAG
     EPPQNSSLAA TYLKLDSAEL DSATVADALR GALVAPVITA HPTETRRRTV FDTQHRITEL
     MRLRLHGQTE TDDGRNINLE LRRHIFTLWQ TALIRLSRLK IQDEIKTGLR YYQAAFLEVI
     PKVNAEVRTA LQARWPEADL LELPILRPGS WIGGDRDGNP NVTADVVRQA TGRASYTAFE
     HYFTEISALE QELSMSARLV KVSDDLAALA DKCHEPARAD EPYRRALRVI HGRLTATAGE
     ILDSQPEHEL DLGLQRYVTP AELLADLDVI DHSLRSNGSG VLADDRLAQL REAVRVFGFH
     LSGLDLRQNS DVHEEVVAEL LAWAGVHADY QSLSEPERVE LLAAELATRR PLTKDDAELS
     ELARKELDIV AAAARAVHVY GPHAIPNYII SMCQSVSDML EAAILLKEVG LLDASGDEPY
     APVGIVPLFE TIDDLQRGSS ILEAVLDLPL YRAVVTARGD SQEVMLGYSD SNKDGGYLAA
     NWALYRAELD LVESARKTGI RLRLFHGRGG TVGRGGGPSY DAILAQPPGA VNGSLRITEQ
     GEVIAAKYAE PRVAHRNLET LLAATLEATL LDVEGLGDAA EPAYEVLDEL AARAQRAYAE
     LVHVTPGFVE YFKASTPVSE IGALNIGSRP TSRKPTTSIS DLRAIPWVLA WSQSRVMLPG
     WYGTGAAFEG WIAEGDGRLE VLQDLYHRWP FFRTVLSNMA QVLSKSDMGL AARYSELVED
     EALRQRVFDK IVDEHDRTIR MHKLITGQDD LLADNPALAR SVFNRFPYLE PLNHLQVELL
     RRYRSGDDDE LVQRGILLTM SGLATALRNS G
//