ID   A4TC23_MYCGI            Unreviewed;       937 AA.
AC   A4TC23;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Mflv_3706 {ECO:0000313|EMBL:ABP46178.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46178.1};
RN   [1] {ECO:0000313|EMBL:ABP46178.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46178.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP46178.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46178.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
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; CP000656; ABP46178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TC23; -.
DR   STRING; 350054.Mflv_3706; -.
DR   KEGG; mgi:Mflv_3706; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
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:ABP46178.1}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
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   937 AA;  103429 MW;  1AC153C494C8F9B3 CRC64;
     MPSSPATPDQ SLEPIGAVQR TQVGREATEP MREDIRLLGT ILGDTVREQN GDEVFDLVER
     ARVEAFRVRR SEIDRADMAK LFDDVDVHRA IPVIRAFTHF ALLANVAEDI HRERRRRIHE
     AAGEPPQDSR LDATYLKLDD AGLDAGAVAD ALAGALVSPV ITAHPTETRR RTVFDTQHRI
     TELMRLRLHG HDTSPDGRDV EQELRRHILT LWQTALIRLS RLKIQDEIET GLRYYEAALF
     EVIPQVNAEV RAALQQRFPE AGLLEQPIVR PGSWIGGDRD GNPNVTAEVV RLATGSAAYT
     ALAHYFAELT GLEQELSMSA RLVHITDELA ALADSCHEPA RADEPYRRAL RVVHARLTAT
     AQQILDRQPE HELDLGMEPY AAPGELLDDL DVIDASLRAN GSAVLADDRL GRLREAVRVF
     GFHLSGLDMR QNSDVHEEVV AELLAWAGVH SDYTSLSEDD RVEVLAAELA TRRPLTSPDA
     DLSELARKEL DIVAAAARAV HVFGPQAVPN YIISMCQSVS DMLEAAILLK EAGLLDASSE
     HPYAPVGIVP LFETIDDLQR GSSILEAALE LPLYRGLVSA RGDSQEVMLG YSDSNKDGGY
     LAANWALYRA ELELVESSRK TGIRLRLFHG RGGTVGRGGG PSYDAILAQP PGAVQGSLRI
     TEQGEVIAAK YAEPRIAHRN LETLLAATLE ATLLDMEGLG DLAGTAYEVL DDLAARAQRA
     YAELVHDTPG FVDYFKASTP VSEIGALNIG SRPTSRKPTT SISDLRAIPW VLAWSQSRVM
     LPGWYGTGTA FEDYVGDGDD AEARLQVLQD LYRRWPFFAT VLSNMAQVLA KSDLGLAAHY
     SELVEDEELR RRVFDKIVDE HARTIRMHRL ITGHEDLLAD NPSLARSVFN RFPYLEPLNH
     LQVELLRRYR SGDEDDLVQR GILLTMSGLA TALRNSG
//