ID   M5B6E4_9MICO            Unreviewed;       910 AA.
AC   M5B6E4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=ppcA {ECO:0000313|EMBL:CCE74311.1};
GN   Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=CMN_00341 {ECO:0000313|EMBL:CCE74311.1};
OS   Clavibacter nebraskensis NCPPB 2581.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE74311.1, ECO:0000313|Proteomes:UP000012170};
RN   [1] {ECO:0000313|EMBL:CCE74311.1, ECO:0000313|Proteomes:UP000012170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA   Gartemann K.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCE74311.1, ECO:0000313|Proteomes:UP000012170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA   Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA   Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA   Eichenlaub R., Rueckert C.;
RT   "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT   nebraskensis.";
RL   Submitted (APR-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; Evidence={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; HE614873; CCE74311.1; -; Genomic_DNA.
DR   RefSeq; WP_015489128.1; NC_020891.1.
DR   AlphaFoldDB; M5B6E4; -.
DR   KEGG; cmc:CMN_00341; -.
DR   PATRIC; fig|1097677.3.peg.288; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000012170; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   910 AA;  99170 MW;  6EB6962CDDB9F374 CRC64;
     MTTPPKKPLP LEHDSTRDGT RDAVEPALRS DVSHLGGLLG QVLRESGGDD LLRDVERLRE
     LVIDAYESAR DASIDDAERL VATFTPERAE QVARAFTCYF HLANLAEEHH RVRVLREREA
     ASGFVPDSIP DAVGKLTEEL GREEAMRRLG EMRFHPVLTA HPTEARRRAV ATGIRRIGDL
     LTERDGAMAG TLTGQDVDRR LLEEIDGLWR TSPLRTTRPT PLDEVRTAMG VFDQTLFEVV
     PRVYRLLDDW LLGDEAGARD AVAPAFFRLG NWIAADRDGN PYVTAAVTEE AAGIASEHIL
     LGLERVALRV GRSLTLGDAD TPPSAELREL AAAQDALAPH LTARIGTRAP AELHRRVLLV
     IAGRLAATRE RHDDPIAYPS AAELLADLRV LQASLRSAGA HRIAGGELQG LVWQAETFGF
     HLAEMEVRQH SQVHREALRE VLAVASADAS GEQAPELAPM TVEVLDVFRT LARLQQRHGV
     APFSRFIVSF TQSADDIRTV HELAALALGS AEEAPVLDVI PLFETFADLN ASTEILDGMI
     RLPQVAARLA QTGRKLEVML GYSDSSKDVG PVSATFALFD AQARIAAWAR ENDIELTLFH
     GRGGALGRGG GPADRAVRAQ PPGSVDGRFK LTEQGEVIFA HYGDKRIAAR HIEQMAAATL
     LASAPSNEER NAAAAHGSAD MVRTMDEASR ARFFELVKAP GFAPWFAQVT PMEEIGLLAL
     GSRPARRGLS VESLEDLRAI PWVFAWTQAR INLTGWFGLG SALAAVGDED VLRKAYDEWP
     LFTSMIDNVE MSLAKTDGRL AERYLALGDR PDLAALVTEE MELTREWVRK ATGRGEILEG
     RPVLRRAVRL RSPYVDALSL LQLRALRALR TAASDATGQA APGQADPTDP DHRLLLLTVN
     GIAAGLQNTG
//