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Database: UniProt
Entry: A0A0B5DBT0_9ACTN
LinkDB: A0A0B5DBT0_9ACTN
Original site: A0A0B5DBT0_9ACTN 
ID   A0A0B5DBT0_9ACTN        Unreviewed;       910 AA.
AC   A0A0B5DBT0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=BJY54_002814 {ECO:0000313|EMBL:MBB4792202.1}, CP978_14605
GN   {ECO:0000313|EMBL:QEV39622.1}, SNOD_14285
GN   {ECO:0000313|EMBL:AJE41083.1};
OS   Streptomyces nodosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE41083.1, ECO:0000313|Proteomes:UP000031526};
RN   [1] {ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA   Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT   "Sequence of the Streptomyces nodosus genome.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJE41083.1, ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE41083.1,
RC   ECO:0000313|Proteomes:UP000031526};
RX   PubMed=26497174;
RA   Sweeney P., Murphy C.D., Caffrey P.;
RT   "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT   antibiotic production.";
RL   Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN   [3] {ECO:0000313|EMBL:QEV39622.1, ECO:0000313|Proteomes:UP000325763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV39622.1,
RC   ECO:0000313|Proteomes:UP000325763};
RA   Lee N., Cho B.-K.;
RT   "Streptomyces genome completion.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MBB4792202.1, ECO:0000313|Proteomes:UP000544950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4792202.1,
RC   ECO:0000313|Proteomes:UP000544950};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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|ARBA:ARBA00001946,
CC         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; CP009313; AJE41083.1; -; Genomic_DNA.
DR   EMBL; JACHMR010000001; MBB4792202.1; -; Genomic_DNA.
DR   EMBL; CP023747; QEV39622.1; -; Genomic_DNA.
DR   RefSeq; WP_043441004.1; NZ_JACHMR010000001.1.
DR   STRING; 40318.SNOD_14285; -.
DR   KEGG; snq:CP978_14605; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000031526; Chromosome.
DR   Proteomes; UP000325763; Chromosome.
DR   Proteomes; UP000544950; 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; 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:AJE41083.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031526}.
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        568
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   910 AA;  101444 MW;  B2F979BB1E23E51D CRC64;
     MSSADDQTTT TNSELRADIR RLGDLLGETL VRQEGPELLE LVERVRRLTR EDGEAAAELL
     RGTELETAAK LVRAFSTYFH LANVAEQVHR GRELRDRRAA EGGVLARTAD RLKDADPEHL
     RETVGHLNVR PVFTAHPTEA ARRSVLNKLR RIAALLETPV LDSDRRRHDI RLAENIDLVW
     QTDELRVVRP EPADEARNAI YYLDELHAGA VGDVLEDLTA ELERVGVKLP DETRPLTFGT
     WIGGDRDGNP NVTPEVTWEV LILQHEHGIN DALEMIDELR GFLSNSIRYT GATEELLQSL
     DTDLELLPEI SPRYKRLNAE EPYRLKVTCV RQKLLHTKER LAKGTPHEPG RDYLGTSDLL
     RDLRLVQTSL RAHRGGLFAD GRLARTIRTL AAFGLQLATM DVREHADAHH HALGQLFDRL
     GEESWRYEDM PREYRHKLLA KELRSRRPLA PTPAPLDEAG ARTLGTFETV KRALEVFGPE
     VIESYIISMC QGADDVFAAA VLAREAGLVD LHAGWARIGI VPLLETTDEL RAADSILEEM
     LADPSYRRLV ALRGDVQEVM LGYSDSSKFG GITTSQWEIH RAQRRLRDVA HRYGVRLRLF
     HGRGGTVGRG GGPSHDAILA QPWGTLEGEI KVTEQGEVIS DKYLIPSLAR ENLELTVAAT
     LQASALHTAP RQSGEALARW DAAMDVVSDA AHAAYRELVE DPGLPAYFFA STPVDQLADL
     HLGSRPSRRP DSGAGLDGLR AIPWVFGWTQ SRQIVPGWYG VGSGLKALRE AGLDTVLAEM
     HEEWHFFRNF VSNVEMTLAK TDLRIARHYV DTLVSEDLRP VFTAIETEHR LTVREVLRIT
     GEKELLDADP VLKQTFAIRD AYLDPISYLQ VALLKRQRDA AAAGAEPDPL LARALLLTVN
     GVAAGLRNTG
//
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