ID A0A132T5M8_9MYCO Unreviewed; 937 AA.
AC A0A132T5M8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ASJ79_24540 {ECO:0000313|EMBL:KWX66679.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX66679.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX66679.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX66679.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWX66679.1}.
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DR EMBL; LMVQ01000182; KWX66679.1; -; Genomic_DNA.
DR RefSeq; WP_067956229.1; NZ_LMVQ01000182.1.
DR AlphaFoldDB; A0A132T5M8; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000070146; Unassembled WGS sequence.
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:KWX66679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT ACT_SITE 164
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 596
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 937 AA; 102895 MW; 726C6E799C32227D CRC64;
MAQPSQARDV TLEPIGAVHR TQVGREATEP MREDIRMLGA ILGDTVREQN GDEVFELVER
ARVEAFRVRR SEIDRADMAK LFDGVDVHLA IPVIRAFTHF ALLANVAEDI HRERRRAVHE
AAGELPQDSS LAATYLKLDD AELDAAAVAE ALVGALVSPV ITAHPTETRR RTVFDTQHRI
TELMRLRLHG FTGTPDGKDI DRELRRHILT LWQTALIRLS RLKIQDEIET GLRYYAAAFL
EVIPQVNAEV RSALQARWPE ASILAEPILR PGSWIGGDRD GNPNVTAEVV RLATGSAAHT
AFAHYFTELT ALEQELSMSV RLVHVSDDLA ALADACHEPA RADEPYRRAL RVVHARLTAT
ARQILDRQPE HELDLGLDPY SAPGELLGDL DAIDASLRAN GSVLLADDRL ARLREAVRVF
GFHLSGLDMR QNSDVHEEVV AELLAWAGVH PDYTALDEQE RVEILAAELA TRRPLTGPDA
ELSELARKEL DIVAAAARAV RVFGPQAVPN YIISMCQSVS DMLEAAILLK EAGLLDASSE
HPHAPVGIVP LFETIDDLQR GASILEAALD LPLYRAVVAA RGDSQEVMLG YSDSNKDGGY
LAANWALYRA ELDLVESARK TGIRLRLFHG RGGTVGRGGG PSYDAILAQP PGAVQGSLRI
TEQGEVIAAK YAEPRIAHRN LETLLAATLE ATLLDVEGLG DAAGPAYQVL DDLAARAQRA
YAELVHETPG FVEYFKASTP VSEIGALNIG SRPTSRKPTT SISDLRAIPW VLAWSQSRVM
LPGWYGTGTA FEEYVGDGPG SDARLAVLQD LYRRWPFFAT VLSNMAQVLA KSDLGLAARY
SELVEDEALR RRVFDKIAAE HARTIRMHEL ITGHDDLLAD NPALARSVFN RFPYLEPLNH
LQVELLRRYR SGDQDELVQR GILLTMSGLA TALRNSG
//
