ID A0A0G3H7X0_9CORY Unreviewed; 923 AA.
AC A0A0G3H7X0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:AKK08855.1};
GN ORFNames=CTEST_07090 {ECO:0000313|EMBL:AKK08855.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08855.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK08855.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08855.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) 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 ---------------------------------------------------------------------------
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; CP011545; AKK08855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3H7X0; -.
DR STRING; 136857.CTEST_07090; -.
DR KEGG; cted:CTEST_07090; -.
DR PATRIC; fig|136857.5.peg.1413; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000035540; Chromosome.
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:AKK08855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035540}.
FT ACT_SITE 142
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 583
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 923 AA; 102824 MW; E96020165655D1F0 CRC64;
MRVTARNHLQ EDIRYLGRIL GQVIAEQEGD EVFNLVELAR QQAFEVAKGN ADLEVLVELF
RNIEPTQATR VIRAFSHFAL MANLAEDIHD DVNRERQLDA GGPALDSTLD ATWDKLASAE
LESADIARIL DGALVAPVLT AHPTETRRRT VFDAQKHITE LLIQRNAVLE AELNARTEAR
LASIDNDIRR RMTILWQTAL IRVARPRIED EIEVGLRYYK LSLLKEIPAL NRAVNQRLKA
DFGDVTPARP ILRPGSWIGG DHDGNPYVTA ETLDYASRRA AQTVLKYYAA QLHALEHELS
LSDRMTGVTV ELVALAKEGN NEVPSRVDEP YRRAVHGVRG RILATTATLV GEDAVEGVWH
RQYAPYTSAE EFDADLATID VSLRSSQDDI IADDRLASIR SAIASFGFHL YSIDLRQNSE
SFENVLTEVF ATAHVTEDYA ALSEDAKVEL LTTELRTPRP LVPRGYRGFS EPTQRELDLI
AQASDSVERF GEKMVPHQII SMATSVSDIL EPMVLLKEAG LIRADGDTPT GSIDIIPLFE
TIDDLEAGAD ILRQLWDLPL YRSYLTQRGG IQEIMLGYSD SNKDGGYFAA NWALYAAELE
LVEISREYGI RLRLFHGRGG TVGRGGGPSY DAILAQPKGA VDGSVRVTEQ GEIISAKYGS
PRAARRNLEA LVSATLEASL LPVDELEDRE RAIEIMTEIS RLSRDKYASL IHEDPGFIPY
FVQSTPLAEI GALNIGSRPT ARKQTKAVDD LRAIPWVLAW SQSRVLLPGW FGVGTALAEW
IGEGEGSEER RAELRRLYET WPFFTSVMSN MAQVMSKAGM ELAELYARLV DDREIASRVH
AVIVEEFELT RRMFSEVTGS DDLLADNPSL ARSVRRRFPY LLPLNIIQLE LLRRHRAGDE
RDAVSRGIQL TMNGLATALR NSG
//
