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
//