ID   A1UFP3_MYCSK            Unreviewed;       946 AA.
AC   A1UFP3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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   OrderedLocusNames=Mkms_2454 {ECO:0000313|EMBL:ABL91651.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL91651.1};
RN   [1] {ECO:0000313|EMBL:ABL91651.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL91651.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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}.
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DR   EMBL; CP000518; ABL91651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UFP3; -.
DR   STRING; 189918.Mkms_2454; -.
DR   KEGG; mkm:Mkms_2454; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
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:ABL91651.1}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        604
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   946 AA;  104886 MW;  73E65D55F5A78AA1 CRC64;
     MRRVRRTPIL ERMADLPEAL EPIGSVTRTE VGREASEPMR EDIRLLGAIL GDTVREQNGE
     DVFDLVERAR VESFRVRRSE IDRAELAGLF DGIGVRAAIP VIRAFTHFAL LANVAEDIHR
     ERRRAVHVAA GEPPQDSSLA ATYAKLDSAQ LDSDEVSAAL SGALVSPVIT AHPTETRRRT
     VFDTQHRITE LMRLRAHGHE TTDDGRDIEL ELRRHILTLW QTALIRLSRL KIQDEIETGL
     RYYRAAFFEV IPRVNAEVRS ALQTRWPDAD LLAEPILRPG SWIGGDRDGN PNVTAEVVRQ
     ATSRAAYTAF EHYFAELTGL EQELSMSARL VHVSDELAAL ADACHEAARA DEPYRRALRV
     IHGRLTATAL EILDNQPEHE LDLGLERYAT PAELLADLDV IDASLRGHGS AVLADDRLLR
     LREAVRVFGF HLSGLDMRQN SDVHEEVVAE LLAWAGVHDD YASLPESDRI DLLVSELATR
     RPLTSQKAEL SELARKELDI VRAGARAVRV FGPQAVPNYI ISMCESVSDM LEAAILLKEA
     GLLDVSDDEP YAPVGIVPLF ETIDDLQRGS SILEAALDLP LYRGMVTARG DSQEVMLGYS
     DSNKDGGYLA ANWALYRAEL DLVESSRKTG IRLRLFHGRG GTVGRGGGPS YDAILAQPPG
     AVNGSLRITE QGEVIAAKYA EPRIAHRNLE TLVAATLEST LLDVEGLGDE AGPAYEVLDD
     LAARAQRAYA ELVHETPGFV DYFKASTPVS EIGALNIGSR PASRKPTTSI SDLRAIPWVL
     SWSQSRVMLP GWYGTGSAFE QYIAEGAAES EDRLGVLQDL YRRWPFFRTV LSNMAQVLAK
     SDLGLAARYS ELVEDEDLRR RVFDKIADEH ERTIRMHRLI TGQDDLLADN PALARSVFNR
     FPYLEPLNHL QVELLRRYRS GEDDELVQRG ILLTMSGLAT ALRNSG
//