ID   K4R8Y7_STRDJ            Unreviewed;       913 AA.
AC   K4R8Y7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:CCK29525.1};
GN   ORFNames=BN159_5146 {ECO:0000313|EMBL:CCK29525.1};
OS   Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK29525.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK29525.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC   {ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA   Pelzer S., Kalinowski J., Mack M.;
RT   "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT   heterologous production of the unique antibiotic roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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; HE971709; CCK29525.1; -; Genomic_DNA.
DR   RefSeq; WP_015659865.1; NC_020504.1.
DR   AlphaFoldDB; K4R8Y7; -.
DR   STRING; 1214101.BN159_5146; -.
DR   KEGG; sdv:BN159_5146; -.
DR   PATRIC; fig|1214101.3.peg.5219; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008043; 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; 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:CCK29525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008043}.
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        571
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   913 AA;  101589 MW;  95F0466017EB2F34 CRC64;
     MSSADDLTTS TTSTSSELRA DIRRLGDLLG ETLVRQEGPD LLDLVERVRR LTREDGEAAA
     ELLRGTELDT AAKLVRAFST YFHLANVTEQ VHRGRELRAK RAAEGGLLAR TADRLKDADP
     EHLRATVRHL NVRPVFTAHP TEAARRSVLN KLRRIATLLE TPVIEADRRR YDTRLAENID
     LVWQTDELRV VRPEPADEAR NAIYYLDELH AGAVGDVLED LTAELERVGV KLPDDTRPLT
     FGTWIGGDRD GNPNVTPQVT WDVLILQHEH GINDALEMID ELRGFLSNSI RYTGATQELL
     DSLAADLERL PEISPRYKRL NAEEPYRLKA TCIRQKLENT KTRLAKGIPH EDGRDYLGTS
     ELLHDLTLIQ TSLREHRGGL FADGRMNRTI RTLAAFGLQL ATMDVREHAD AHHHALGQLF
     DRLGEESWRY TDMPRDYRAK LLAKELRSRR PLAPTPAPVD AAGEKTLGVF QTVKRALEVF
     GPEVIESYII SMCQGADDVF AAAVLAREAG LVDLHAGWAK IGIVPLLETT DELKAADTIL
     EDMLSDPSYR RLVALRGDVQ EVMLGYSDSS KFGGITTSQW EIHRAQRRLR DVAHRYGVRL
     RLFHGRGGTV GRGGGPSHDA ILAQPWGTLE GEIKVTEQGE VISDKYLVPS LARENLELTV
     AATLQASALH TAPRQSDEAL ARWDAAMDVV SDAAHAAYRR LVEDPDLPTY FLASTPVDQL
     ADLHLGSRPS RRPGSGVSLD GLRAIPWVFG WTQSRQIVPG WFGVGSGLKA LREAGLDTVL
     DEMHEQWHFF RNFVSNVEMT LAKTDLRIAQ HYVDTLVPDE LKHVFDTIKA EHELTVREVL
     KVTGETELLD ATPALRQTFS IRDAYLDPIS YLQVALLKRQ RDAAAAGEQA DPLLSRALLL
     TVNGVAAGLR NTG
//