ID   F6FW45_ISOV2            Unreviewed;       919 AA.
AC   F6FW45;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-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=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Isova_2904 {ECO:0000313|EMBL:AEG45589.1};
OS   Isoptericola variabilis (strain 225).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN   [1] {ECO:0000313|EMBL:AEG45589.1, ECO:0000313|Proteomes:UP000009236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Isoptericola variabilis 225.";
RL   Submitted (MAY-2011) 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; CP002810; AEG45589.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6FW45; -.
DR   STRING; 743718.Isova_2904; -.
DR   KEGG; iva:Isova_2904; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000009236; 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};
KW   Pyruvate {ECO:0000313|EMBL:AEG45589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009236}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        569
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   919 AA;  100778 MW;  4D5BD86169F011D7 CRC64;
     MSENQAQPTG VVTDPSPASA GARERVVARH EMPDPLRDDI RLLGGLLGTV LREAGGQDLL
     DDVERLRELT IRAYGSDDGG TALAEAADLV AGFPLERAEQ VARAFTCYFH LANLAEEYHR
     VRVLRQRETE AGAAVDESLP HAFTQLAEEV GRDEALRRLS ELEFRPVLTA HPTEARRRAV
     SGAVRRISNL LAERDTMRPG GTSLVENERR LLAEIDTMWR TSPIRAAKPT VLDEVKTAMG
     VFDATLFNTF PEVYRRLDDW LLDGDAGRAA PVARPFVFLG SWIGGDRDGN PNVTAEVTRQ
     AATLAAEHAL TALEEAARQV GRKLTLDEAG TPPSSALKAL WQRLRQLSED LTAQAAAVSP
     REPHRAAVLA IAGRIGATRR RDADLAYRRP EELEAELRVV QDSLVEAGAP RAAYGDLQKL
     VWQVQTFGFH LAEIEVRQHS QVHAAALDEI AEKGVHGDLS DRTREVLDTF RALGAVQRRF
     GERAARRYIV SFTQAPEHLA AVYHLAELAF EDAEDIPVID AIPLFETFAD LEASVDILEA
     ALELPQVQRR LAANGRRVEV MLGYSDSSKD VGPVAATLAL HSAQSRIAEW ARRHDITLTL
     FHGRGGALGR GGGPANRAVL AQPPHSVDGR FKLTEQGEVI LARYGDPTIA ARHIEQVAAA
     TLLASAPSTE KRNAATAERF AHVASSLDAS SRARFHALVK SEGFPQWFAQ VTPLEEIGLL
     PIGSRPAKRG LSVNSLDDLR AIPWVFSWSQ ARINLAGWFG LGTALREFGD SPERIAELQA
     AYREWPLFAT LLDNVEMSLA KTDERIAAQY LALGDRDDLA QMVLDELRLT REWVLRVTGN
     EWPLANRRVL GRAVQLRSPY VDALSLLQVR ALRALRTEGA SEGVTAESGK WVDGGYKDRW
     QHLLLLTVNG VSAGLQNTG
//