ID A0A1M7F1Y9_9ACTN Unreviewed; 917 AA.
AC A0A1M7F1Y9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216499_107170 {ECO:0000313|EMBL:SHL98112.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHL98112.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHL98112.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHL98112.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRBI01000007; SHL98112.1; -; Genomic_DNA.
DR RefSeq; WP_073497859.1; NZ_FRBI01000007.1.
DR AlphaFoldDB; A0A1M7F1Y9; -.
DR STRING; 310782.SAMN05216499_107170; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000184111; 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:SHL98112.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184111}.
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 575
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 917 AA; 101043 MW; C0558462CFA39FCF CRC64;
MSSADTAPDS STASSTALRA DIRRLGELLG GTLVRQEGQD LLDLVEKVRA LTRSDGEAAA
ALLGDTDLET AAKLVRAFST YFHLANVTEQ VHRGRELRSR RAVEGGLLAQ TADLLKEGDA
EHVRESVRNL NVRPVFTAHP TEAARRSVLN KLRRIAELLE QDGQGEGSTG DRRRADLRLA
ENIDLLWQTD ELRVVRPEPA DEARNAIYYL DELHAGAVGD VLEELAAELE RVGVPLPPQT
RPLTFGTWIG GDRDGNPNVT PEVTWDVLIL QHEHGITDAL QLVDFLRGAL SNSIRNSGAS
SELLDSLATD LVALPEISPR YKRLNAEEPY RLKATCIRQK LINTRERLAA GTPHVPGRDY
LGTAGLLDDL QQIQASLRAH RGGLIADGRM DRTIRTLSAF GLQLATMDVR EHAEAHHHAL
GQLFDRLGEE SWRYADMPRD YRRKLLAKEL RSRRPLAPTP APLDEAGAKT LGVFHTIREA
FERFGPEVVE SYIISMCLGS DDVFAAAVLA REAGLIDLHT GVARIGIVPL LETTDELKIA
DKLLDEMLSD PSYRRLVSLR GDVQEVMLGY SDSSKFGGIT TSQWEIHRAQ RRLRDVAHRH
GVRLRLFHGR GGTVGRGGGP SHTAILAQPW GTLEGEIKVT EQGEVISDKY LIPSLARENL
ELTVAATLQA SALHTSPRQS DEALTRWDAA MDIVSEAAHG AYRKLVEDPD LPPYFFASTP
VDQLGELHLG SRPSRRPDSG AGLDGLRAIP WVFGWTQSRQ IVPGWYGVGT GLKAAREAGL
DSVLEEAHGQ WHFFRNFLSN VEMTLAKTDL RIARHYVETL VPDELRHVFE TIEAEHELTV
REVLRLTGES ELLAASSVLA QTFHIRDQYL DPISYLQVTL LARQRAAAAS GEEPDPLLSR
ALLLTVNGVA AGLRNTG
//
