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Database: UniProt
Entry: A0A1I5BZW3_9ACTN
LinkDB: A0A1I5BZW3_9ACTN
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ID   A0A1I5BZW3_9ACTN        Unreviewed;       860 AA.
AC   A0A1I5BZW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN04489713_10391 {ECO:0000313|EMBL:SFN80300.1};
OS   Actinomadura madurae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=1993 {ECO:0000313|EMBL:SFN80300.1, ECO:0000313|Proteomes:UP000183413};
RN   [1] {ECO:0000313|EMBL:SFN80300.1, ECO:0000313|Proteomes:UP000183413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43067 {ECO:0000313|EMBL:SFN80300.1,
RC   ECO:0000313|Proteomes:UP000183413};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|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}.
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DR   EMBL; FOVH01000003; SFN80300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5BZW3; -.
DR   STRING; 1993.SAMN04489713_10391; -.
DR   eggNOG; COG2352; Bacteria.
DR   InParanoid; A0A1I5BZW3; -.
DR   Proteomes; UP000183413; 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; 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};
KW   Pyruvate {ECO:0000313|EMBL:SFN80300.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183413}.
FT   ACT_SITE        134
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        523
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   860 AA;  94649 MW;  867DA13A2B4C257E CRC64;
     MPEPLRRDVR LLGAMLGDSL VEYGGTGLLD DVERLRRAVI AARRGETGIE EVAALVDGWS
     LERAGQVARA FTVYFHLTNL AEEHHRIRTL RERDTGDTVP GSAAAAIEEI RASGDGRLDA
     IIEGLEFRPV FTAHPTEARR RAVVTAIQRI SDLLARLNAG PGASERQETE RSLREEIDLL
     WRTALRRGTQ IDPLDEVRTA MAAFDETIFR VVPAVYRALD RALDGERTGT RPPKARPYLR
     FGSWIGGDRD GNPYVTAQVT RDAVMIQADH VLRALENACA RVGRELTVHE STTPPSKDLL
     NALAAARTAH PSRLREIAER SPGEEHRQLL LYAAARIAAT RERDADLAYA SPDELLADLR
     TVQDSLAGAG ATRQAYGRVQ QLVWQVETFG FHLAELEIRQ HSELHEKALA ELDGDHSEMT
     DEILDTLRTV AWIQNRFGVR ACHRYIVSFT RSAADIANVH ELAASLGDGA PVLDVIPLFE
     TGEDLERAPS VLDGMLEIPA VRRRLDETGR RLEVMLGYSD SAKQLGPTSA TLHLYDTQEA
     LTAWAARHDI TLTLFHGRGG SLGRGGGPAN RAILAQAPGS VAGRFKVTEQ GEVIFARYGH
     AEIAKRHVEQ VTSAVLLAST DPVQDRAREA AARFRPLADK IGEAAEAAFR SLVETDGFAA
     WFARVSPLEE ISELRIGSRP ARRKAARGLE DLRAIPWVFA WTQTRVNLPG WYGLGSGLAA
     VSDDGRDLTG LREAYEAWPL FNTLLDNAEM SLAKSDRAIA ERYLALGERP ELSAAVLAEY
     DRTHRLVLAV TGHDRLLENR RVLSRAVELR NPYVDALSHL QLRALKALRA GVDDEDERTH
     LESLLLLSVN GVAAGLQNTG
//
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