ID A0A0E3XSU8_MYCCH Unreviewed; 929 AA.
AC A0A0E3XSU8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=GR01_23130 {ECO:0000313|EMBL:AKC40893.1};
OS Mycobacteroides chelonae (Mycobacterium chelonae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=1774 {ECO:0000313|EMBL:AKC40893.1, ECO:0000313|Proteomes:UP000033056};
RN [1] {ECO:0000313|EMBL:AKC40893.1, ECO:0000313|Proteomes:UP000033056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35752 {ECO:0000313|EMBL:AKC40893.1,
RC ECO:0000313|Proteomes:UP000033056};
RX PubMed=26021923;
RA Hasan N.A., Davidson R.M., de Moura V.C., Garcia B.J., Reynolds P.R.,
RA Epperson L.E., Farias-Hesson E., DeGroote M.A., Jackson M., Strong M.;
RT "Draft Genome Sequence of Mycobacterium chelonae Type Strain ATCC 35752.";
RL Genome Announc. 3:e00536-15(2015).
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; CP010946; AKC40893.1; -; Genomic_DNA.
DR RefSeq; WP_046255302.1; NZ_MLCH01000004.1.
DR AlphaFoldDB; A0A0E3XSU8; -.
DR GeneID; 31682256; -.
DR PATRIC; fig|1774.35.peg.4702; -.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000033056; 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:AKC40893.1}.
FT ACT_SITE 159
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 591
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 929 AA; 103127 MW; 2AAFB0360CFE4C0A CRC64;
MAEVTDLAPI GAVTRTQVGR EATEPMREDI RLLGTILGLT VREQCGDEVF ELVERARVES
FRVRRSEIDR AELAQLFDGV DIHRAIPVIR AFTHFALLAN VAEDIHRERR RAVHVAAGAP
PQDSSLAATY LKLDAAQLSS DRVAHALTGA LVSPVITAHP TETRRRTVFD TQHRITELMR
LRMQGLSQTE SGRNIEHELQ RHILTLWQTA LIRLSRLKIQ DEIAVGLRYY QASFFEVIPE
INAEIRTALR RRWPDAELLS EPILRPGSWI GGDRDGNPNV TAEVVHLATS SAAQTAIAYY
FEQLVALEQE LSLSVRLVTV SADLLALAEQ GRETDRADEP YRRALRVIHA RLTATAANIL
DQLPEHGLDL DLIPYRTPDE LLRDLDIVDA SLRAHGSVVL ADDRLRALRE SIHVFGFHLS
GLDMRQNSDV HEEVVSELLA WAGVHSDYRS LSEQQRIEVL VTELRTRRPL IGEGAELSEL
ARKELDIVAA AARAVQTYGP RAVPNYIISM CQSVSDMLEA AILLKEAGLL DASRPRPFCP
VGIVPLFETI DDLQRGSAIL EAALELPLYR ALVAARGESQ EVMLGYSDSN KDGGYLAANW
ALYRAELDLV ESARRNGIRL RLFHGRGGTV GRGGGPSYDA ILAQPPGAVS GSLRITEQGE
VIAAKYAEPR AAHRNLETLL AATLESTLLD VEGLGEAAGA AYEILDDLAA RAQRTYRELV
HETPGFVEYF KASTPVNEIG ALNIGSRPTS RKPTTSIADL RAIPWVLAWS QSRVMLPGWY
GTGAAIEQWI AEGDGRLEVL QQLYRRWPFF QTVLSNMAQV LAKSDMGLAS RYAELVDDET
LRHRVFDKIV AEHDRTIAMH QLITGHEDLL ADNPALARSV FNRFPYLEPL NHLQVELLRR
YRSGDQDELV QRGILLTMSG LATALRNSG
//
