ID   B0REE4_CLAMS            Unreviewed;       910 AA.
AC   B0REE4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
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:CAQ02036.1};
GN   OrderedLocusNames=CMS1939 {ECO:0000313|EMBL:CAQ02036.1};
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ02036.1, ECO:0000313|Proteomes:UP000001318};
RN   [1] {ECO:0000313|EMBL:CAQ02036.1, ECO:0000313|Proteomes:UP000001318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1
RC   {ECO:0000313|Proteomes:UP000001318};
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ02036.1; -; Genomic_DNA.
DR   RefSeq; WP_012299267.1; NC_010407.1.
DR   AlphaFoldDB; B0REE4; -.
DR   STRING; 31964.CMS1939; -.
DR   KEGG; cms:CMS1939; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000001318; 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;  99150 MW;  69668577C945F33E CRC64;
     MTTPPKKPLP LEHDSTRDGT RDAVEPALRS DVSHLGGLLG QVLRESGGED LLRDVERLRE
     LVIDAYESAR DASIDDAERL VATFTPERAE QVARAFTCYF HLANLAEEHH RVRVLREREA
     AAGFVPDSIP DAVGTLTEEL GREEAMRRLG EMRFHPVLTA HPTEARRRAV ATGIRRIGDL
     LTERDGAMAG TLTGADIDRR LLEEIDGLWR TSPLRTTRPT PLDEVRTAMG VFDQTLFEVV
     PRVYRLLDDW LLGEEAGVRD AVAPAFFRLG NWIAADRDGN PYVTAAVTEE AAGIASEHIL
     LGLERVALRV GRSLTLGDAD TPPSPELREL AAAQDALAPH LTARIGTRAP AELHRRVLLV
     IAGRLAATRE RHDDPIAYPS AAELLADLRV LQGSLRSAGA HRIAGGELQG LIWQAETFGF
     HLAEMEVRQH SQVHREALRE VLAVAAADAS GDAVPELAPM TVEVLYVFRA LARLQERHGV
     APFCRFIVSF TQSADDIRTV HELAALALGS AEDAPVLDVI PLFETFADLN ASTEILDGMI
     RLPQVAARLE QTGRKLEVML GYSDSSKDVG PVSATFALFD AQARIAAWAR ENDIELTLFH
     GRGGALGRGG GPADRAVRAQ PPGSVDGRFK LTEQGEVIFA HYGDKRIAAR HIEQMAAATL
     LASAPSNEER NAAAAQGSAE MVRTMDEASR ARFFELVKAP GFAPWFTQVT PMEEIGLLAL
     GSRPARRGLS VESLEDLRAI PWVFAWTQAR INLTGWFGLG SALAAVGDEA VLRKAYDEWP
     LFTSMIDNVE MSLAKTDGRL AERYLALGDR PDLAALVTEE MELTREWVRK ATGRGDILEG
     RPVLRRAVRL RSPYVDALSL LQLRALRALR TTASAATGQA APGQADPTDP DHRLLLLTVN
     GIAAGLQNTG
//