ID X8CH68_MYCIT Unreviewed; 938 AA.
AC X8CH68;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ECO:0000313|EMBL:EUA55171.1};
GN ORFNames=I550_3322 {ECO:0000313|EMBL:EUA55171.1};
OS Mycobacterium intracellulare 1956.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA55171.1, ECO:0000313|Proteomes:UP000020825};
RN [1] {ECO:0000313|EMBL:EUA55171.1, ECO:0000313|Proteomes:UP000020825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1956 {ECO:0000313|EMBL:EUA55171.1,
RC ECO:0000313|Proteomes:UP000020825};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-2013) 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:EUA55171.1}.
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; JAOG01000002; EUA55171.1; -; Genomic_DNA.
DR AlphaFoldDB; X8CH68; -.
DR PATRIC; fig|1299331.3.peg.3240; -.
DR Proteomes; UP000020825; 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:EUA55171.1}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 938 AA; 102846 MW; 5BA3EAF6CEDCF0C6 CRC64;
MADASEAPED TLEPIGAVQR TPVGREATEP MRADIRLLGA ILGDTVREQN GREVFELVER
ARVESFRVRR SEIDRAELAR MFFRIDIHQA IPVIRAFSHF ALLANVAEDI HRERRRAVHV
AAGEPPPDST LAATYAKLDE AQLDSDTVAD ALKGAVVAPV ITAHPTETRR RTVFVTQHRI
TELMRLHAEG HAETDDGRNI ELELRRQVLT LWQTALIRLS RLQITDEIEV GLRYYAAAFF
KVIPQVNAEV RDALRARWPD ADLFDEPMLQ PGSWIGGDRD GNPNVTADVV RQATGSAAFT
ALAHYLAELT ALEQELSMSA RLVSVTPALT ELAGGCAEKA RADEPYRRAV RVIRARLSAT
SAAILDRTPQ QVLDLGLPPY ETPAELGADL DTIDESLRGH GSALLADDRL ALLREGVRVF
GFHLCGLDMR QNSDAHEEVI CELLAWAGVH PDYRSLPEDE RVELLAAELG TRRPLVADDA
QLSDLARGEL GVVRAAAHAI KRYGPSAVPN YVISMCRSVS DVLEAAILLK EAGLIDASGP
EPYCPVGISP LFETIDDLHN GATILHAILE LPIYRALVAA RGETQEVMLG YSDSNKDGGY
LASSWAVYRA ELALVEVARK TGIRLRLFHG RGGTVGRGGG PSYEAILAQP PGAVNGSLRL
TEQGEVIAAK YAEPQAAQRN LESLLAATLE STLLDVEGLG DAAEPAYAVL DEVAVLAQRA
YAELVHDTPG FVDYFMASTP VSEIGSLNIG SRPTSRKPTE SISDLRAIPW VLAWSQSRVM
LPGWYGTGSA FEQWIAAGPQ SEAERVSILH DLYQRWPFFR SVLSNLAQVL AKSDLGLAAR
YAELVDDEEL RRRVFDKIVD EHGRTIAMHK LITGQDNLLA DNPALARSVF NRFPYLEPLN
HLQVELLRRY RSGDDDELVQ RGILLTMNGL ASALRNSG
//
