ID A0A1J1EPC6_LYSEN Unreviewed; 923 AA.
AC A0A1J1EPC6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:BAW00092.1};
GN ORFNames=LEN_4604 {ECO:0000313|EMBL:BAW00092.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:BAW00092.1, ECO:0000313|Proteomes:UP000218824};
RN [1] {ECO:0000313|Proteomes:UP000218824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M497-1 {ECO:0000313|Proteomes:UP000218824};
RA Takami H., Toyoda A., Uchiyama I., Itoh T., Takaki Y., Arai W., Nishi S.,
RA Kawai M., Shinya K., Ikeda H.;
RT "Complete genome sequence and expression profile of the commercial lytic
RT enzyme producer, Lysobacter enzymogenes M497-1.";
RL DNA Res. 0:0-0(2016).
RN [2] {ECO:0000313|EMBL:BAW00092.1, ECO:0000313|Proteomes:UP000218824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M497-1 {ECO:0000313|EMBL:BAW00092.1,
RC ECO:0000313|Proteomes:UP000218824};
RX PubMed=28065880; DOI=.1093/dnares/dsw055;
RA Takami H., Toyoda A., Uchiyama I., Itoh T., Takaki Y., Arai W., Nishi S.,
RA Kawai M., Shinya K., Ikeda H.;
RT "Complete genome sequence and expression profile of the commercial lytic
RT enzyme producer Lysobacter enzymogenes M497-1.";
RL DNA Res. 24:169-177(2017).
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; AP014940; BAW00092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1EPC6; -.
DR KEGG; lem:LEN_4604; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000218824; 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:BAW00092.1}.
FT ACT_SITE 165
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 584
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 923 AA; 100532 MW; E0C520CB3CA80DCD CRC64;
MTDSSDEPLR AAEWAEQAAE RAADFAPTDA LLREDVKTLG ALVGEILAEQ RGQGFLDGVE
RLRRAAIRRR EAGEPIDALA AALVDIDLEQ AADLVRAFAT YFQAVNLAER VHRIRRRRDY
ERSGAGAQPG GLRDALATLA RQGVSAEEVA ALLPRLRIEP VFTAHPTEAV RRALLEKERT
IVECLVADID RGRTPPERRA DRERIRLALT ASWQTAEAPA AKPSVADEFE HVGFYLSDVL
YRVLPVYYEV FEEALRETYG GAPALPDVLG FGTWVGGDMD GNPNVGADTI AATLAGQRAL
VLAAYRRDLA SLEELLSQSV HRVRVDDAVL AKVEDYRYLL PKAAALLKPR HADMPYRNLL
GLMSARLQAT LEESVHGYPD AAAFLADIDL IERSLAAHQG AHAGGFAVRR LRRRAECFGF
HLAGLDLRQD SATHDAALAA LFEQPEWAAL DVAARAARLH QLLDGEAPPA RPAAAAAQPT
LDVFRAVARL RPRFGARAFG PYIVSMSRSA ADALAVLALA RTAGCADDKG RVPLDVAPLF
ETVDDLDAAA DTLRALFSDP VYRDHLCSRG DRQVVMLGYS DSAKDGGMVA SRWALQQTQI
ALTALAADSG VRIAFFHGRG GSISRGGGKT ERAVIAAPRG SVDGYLRLTE QGEVIHRKYG
IRALALRNLE QTSGAVLRAT LRPRAPEPRE AGWRRIAGEL AGEARAHYRA LVHEDPQFPA
YFRAATPIDV IERLRIGSRP AKRAGSGDIS SLRAIPWVFA WSQNRAGLTA WYGVGTGLAA
ALDRHGRDTL AEMARDWPFF GTLIDDLEMV LAKSDPAIFE RYSQLASALP DGDLHARFHP
SIAAEFERTR DAVLAIKGSD ELLRGDHRLR QSIRLRNPYV DPISLLQVDL LARWRAADRP
DDALLQALVA TVNGIAAGVQ NTG
//
