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Database: UniProt
Entry: A0A2A3I3A8_9ACTN
LinkDB: A0A2A3I3A8_9ACTN
Original site: A0A2A3I3A8_9ACTN 
ID   A0A2A3I3A8_9ACTN        Unreviewed;       935 AA.
AC   A0A2A3I3A8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=BX265_2870 {ECO:0000313|EMBL:PBC78111.1};
OS   Streptomyces sp. TLI_235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC78111.1, ECO:0000313|Proteomes:UP000218662};
RN   [1] {ECO:0000313|EMBL:PBC78111.1, ECO:0000313|Proteomes:UP000218662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TLI_235 {ECO:0000313|EMBL:PBC78111.1,
RC   ECO:0000313|Proteomes:UP000218662};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2017) 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:PBC78111.1}.
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DR   EMBL; NSGV01000001; PBC78111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3I3A8; -.
DR   Proteomes; UP000218662; 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:PBC78111.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218662}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   935 AA;  103581 MW;  5472C76C4227B648 CRC64;
     MTAPVPASAD NPSATAGPDA DNAALRADIR RLGDLLGETL VRQEGPELLG LVEQVRLLSR
     TDGEATAELL AGIDLETAGK LVRAFSTYFH LANVTEQVHR GREFATRRAR EGSLLAQTAD
     QLAEADPKHL QDTLAHLAVR PVFTAHPTEA ARRSVLNKLR RIGELLERIH REHIASGLSE
     ADPVRHSSAK RQADRRLAEV IDLLWQTDEL RIARPEPTDE ARNAVYYLDE LYREAVPAVL
     EELHEELARV GLTLPDGVRP LTFGTWIGGD RDGNPNVTPQ VTWDVLNLQH EYGIKDALAT
     VDDLRNSLST SVRLAGASEE LLASLDADLK ALPELSPRYK RMNAEEPYRL KATCVRLKLE
     NTRDRLAAGT PHVEGRDYVG TRELVADLRL IQDSLRAHRG ELIADGRLAR AIRTVEAFGL
     QLATMDVREH AEAHHHALGQ LFDRLGEEAW RYADMPREYR QRLLAKELRS RRPLAPVPAP
     LDAAGAKTLG VFNTIREGFD RFGDEIVESY IISMCQGADD VFAAAVLARE AGLIDLHAGI
     AKIGIVPLLE TTDELQQADR ILDEMLSDPS YRLLVSLRGD IQEVMLGYSD SSKFGGITTS
     QWEIHRAQRR LRDVAHRYGI RLRLFHGRGG TVGRGGGPSH EAILAQPWGT LEGEIKVTEQ
     GEVISDKYLL PSLARENLEL TVSATLAASA LHTAPRQAPE ELARWDAAMD HVSEAAHTAY
     RALVEQEDLP KYFFAATPVD QLASLHLGSR PSRRPDSGAG LDGLRAIPWV FGWTQSRQIV
     PGWYGVGSGL AAAREAGLGG VLDEMYGQWH FFRNFLSNVA MTLAKTDLRI ARHYVEQLVP
     ADLHHVFDQI TTEHQRTLRE VLRLTGEDEL LDHNPVLKQT FAVRDAYLDP ISYLQVALLR
     RQRDEATKGL TEDPLRARAL LLTVNGIAAG LRNTG
//
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