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,
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; 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
//
