ID H0QZE3_9ACTN Unreviewed; 947 AA.
AC H0QZE3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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 ECO:0000313|EMBL:GAB18194.1};
GN ORFNames=GOEFS_049_00150 {ECO:0000313|EMBL:GAB18194.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB18194.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB18194.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB18194.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) 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:GAB18194.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAEH01000049; GAB18194.1; -; Genomic_DNA.
DR RefSeq; WP_007317531.1; NZ_BAEH01000049.1.
DR AlphaFoldDB; H0QZE3; -.
DR STRING; 1077974.GOEFS_049_00150; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000035034; 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:GAB18194.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT ACT_SITE 172
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 609
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 947 AA; 103565 MW; 9676AA151A1E5D91 CRC64;
MNDPGTFAPT PGSSQWRPAT SIVDHIAVDD AGRALTEPLR DDIRLLGGML GDVVREHSGT
EIFDLIEAAR KAAFAIRRSE IDRDDLAALF DDRPASELLP VVRAFSLFAL LANLGEDQHR
ERRRAIHERG NDVPQASSLA ATYAKLAAAG LTDEQVGTGL AQATVVPVIT AHPTETRRRT
VFEAQNRITE LMRLRRRTEL TPAEERTAIE AIGRQILTLW QTALVRLERL TISDEVASGL
RYYDASFFDV VPTINTEVRR ALLAQYPTSG IADAPMVRMG SWIGGDRDGN PYVTAEIVTL
ATTSAARAAI RHHLDELSSL AQELSMSARL ITVTDDLAVL SSWTLPGGGG GGDEPFRAAI
TKIRSRLAAT GEVMFGEDFL TTDDAPASAA DAYVEASELR ADLDVIDRAL RANNDDAIAD
DRLLRLREGV RTFGFNLSGL DMRQNSDVHE EVVAELLAWA GVNDDYTSLD ESERVAILSA
ELSARRPLLS PDAQLSELAA KEVAIVRAGA RAIKTFGAET IPNYIISMCT SVSDMLEALI
LLKEAGIFDP NDGNPRSTVR VVPLFETIED LQQGSHTLLA VLDVPIYRAL VEAQGGLQEV
MLGYSDSNKD GGYLAANWAL YRAELDLVEA ARKAQIRLRL FHGRGGTVGR GGGPSYDAIL
AQPPGAVQGS LRITEQGEII AAKYAEPVTA HRNLETLLAA TIESSLLDTE GLGDESDDAY
KILDDLAASA RDAYSELVHR TTGFVEYFTS STPLSEIGEL NIGSRPASRK QTKAISDLRA
IPWVLSWSQS RVMLPGWYGT GAAFESWIGD DAERLATLQR YYRTWPFFNS VLSNMAQVMA
KSDLGVAQRY SQLVADDDLR ERVFGKIVEE HERCLRMLAA ITGSDDLLAD NAALKRSVYN
RFPYLEPLNL LQVELLKRYR NGDESREVRR GILLTMNGLA TALRNSG
//
