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Database: UniProt
Entry: A0A086N1T3_9ACTN
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ID   A0A086N1T3_9ACTN        Unreviewed;       911 AA.
AC   A0A086N1T3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=FM21_02830 {ECO:0000313|EMBL:KFG75101.1};
OS   Streptomyces mutabilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG75101.1, ECO:0000313|Proteomes:UP000029095};
RN   [1] {ECO:0000313|EMBL:KFG75101.1, ECO:0000313|Proteomes:UP000029095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM45540 {ECO:0000313|EMBL:KFG75101.1,
RC   ECO:0000313|Proteomes:UP000029095};
RA   Luo X., Zhang L.;
RT   "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL   Submitted (MAY-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFG75101.1}.
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DR   EMBL; JNFQ01000001; KFG75101.1; -; Genomic_DNA.
DR   RefSeq; WP_043372187.1; NZ_KN039946.1.
DR   AlphaFoldDB; A0A086N1T3; -.
DR   STRING; 1915400.FM21_02830; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000029095; 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:KFG75101.1}.
FT   ACT_SITE        137
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,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   911 AA;  101138 MW;  52C385FB2DECB0DB CRC64;
     MSSADDQTTT TTSSELRADI RRLGDLLGET LVRQEGPELL ELVEKVRRLT REDGEAAAEL
     LRGTELETAA KLVRAFSTYF HLANVTEQVH RGRELGAKRA AEGGLLARTA DRLKDADPEH
     LRETVRNLNV RPVFTAHPTE AARRSVLNKL RRVAALLDTP VNEADRRRLD TRLAENIDLV
     WQTDELRVVR PEPADEARNA IYYLDELHLG AVGDVLEDLT AELERAGVKL PDDTRPLTFG
     TWIGGDRDGN PNVTPQVTWD VLILQHEHGI NDALEMIDEL RGFLSNSIRY AGATEELLTS
     LQADLERLPE ISPRYKRLNA EEPYRLKATC IRQKLENTKQ RLAKGTPHED GHDYLGTAEL
     LADLRIIQTS LREHRGGLFA DGRLARTIRT LAAFGLQLAT MDVREHADAH HHALGQLFDR
     LGEESWRYAD MPREYRTKLL AKELRSRRPL APTPAPVDAA GEKTLGVFQT VKRALEVFGP
     EVIESYIISM CQGADDVFAA AVLAREAGLI DLHAGWAKIG IVPLLETTDE LKAADTILED
     LLADPSYRRL VALRGDVQEV MLGYSDSSKF GGITTSQWEI HRAQRRLRDV AHRYGVRLRL
     FHGRGGTVGR GGGPTHDAIL AQPWGTLEGE IKVTEQGEVI SDKYLIPTLA RENLELTVAA
     TLQASALHTA PRQSDEALAR WDAAMDVVSD AAHCAYRGLV EDPDLPAYFF ASTPVDLLGS
     LHLGSRPSRR PDSNAGLDGL RAIPWVFGWT QSRQIVPGWY GVGSGLKALR EAGLDTVLDE
     MHQQWHFFRN FISNVEMTLA KTDLRIAQHY VDTLVPDELK HVFDTIKAEH ELTVAEVLRV
     TGESELLDAD PVLKQTFTIR DAYLDPISYL QVALLGRQRE AAAAGQEADP LLDRALLLTV
     NGVAAGLRNT G
//
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