ID C2ENB5_9LACO Unreviewed; 906 AA.
AC C2ENB5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
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:EEJ71919.1};
GN ORFNames=HMPREF0548_1161 {ECO:0000313|EMBL:EEJ71919.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ71919.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ71919.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ71919.1,
RC ECO:0000313|Proteomes:UP000005583};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ71919.1}.
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DR EMBL; ACGU01000055; EEJ71919.1; -; Genomic_DNA.
DR RefSeq; WP_007125689.1; NZ_GG693253.1.
DR AlphaFoldDB; C2ENB5; -.
DR STRING; 525365.HMPREF0548_1161; -.
DR PATRIC; fig|525365.8.peg.169; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000005583; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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}; Kinase {ECO:0000313|EMBL:EEJ71919.1};
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:EEJ71919.1};
KW Transferase {ECO:0000313|EMBL:EEJ71919.1}.
FT ACT_SITE 138
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 906 AA; 103729 MW; 5ACC50DE8BFE86B0 CRC64;
MTVKKLENNS DVNAMADEVK ILTNLLNEST EQLVGEDAFA KIQNLVKISA AQGQEKLKKQ
IAGLNNQEMI VVARYFATLP LLINISEDVE FASKVNLLNN THQDYLGKLK DTIDIVAKKK
NAEEILEHVN VVPVLTAHPT QVQRKTVLEL TDNIHQLLRS YREVNNGTID RDEWTEQLRA
CIEILMQTDI IRGHKLKVAN EITNVLTYYT KALIPAITKF TTRYKELAQE HGLNVSKATP
ITMGMWIGGD RDGNPYVTAD TLELSATLQS RVIFEYYIKK INELYRTISL STSYMKPSAA
VSNLSELSND DSPFRVNEPY RRAFYYIQSR LVHTEQKLLN ITNINTFLKE RDLENLNKIP
AYQNAQEFKA DLEVIKTSLE ENHDQAVVKT GFTQILEAID IFGFYLATID MRQDSSINEA
CVAELLKSAG ICDHYSDLNE KEKVSLLLKE LNDDPRNLHA NNQPKSELLQ KELKIYKTAR
QLKDRLGEDV IKQHIISHTE SVSDMLEQAV MLKEYDLLDN QKARIQVVPL FETVEDLNNA
RDIIKEYLNF DIVKKWLKSQ NNYQEIMLGY SDSNKDGGYL ASCWNLYKAQ KDLTAIGEDL
GIKITFMHGR GGGPSYEAIT AQPFKSINDR IRMTEQGEII QNKYGNKDTA YYNLEMLASA
TIDRMASKQI VSEDHIDEFR SSMDKIVTES NEVYRKLVFD NPNFIKYFFQ ATPIKEVSKL
NVGSRPASRK KLTDFSGLRA IPWVFSWSQS RVMFPGWYGV GSAFKDFIDS DPDNLKELQD
MYKGWPFFHS LLSNVDMVLS KSNMEIAKQY ADLCEGENVK SVFDIIYKEW QLTKQVILQI
EGHNELLEDN PALKKSLDYR MPYFNILNYI QLEMIKRDRT EEVQGVYESI IPITINGVAS
GLRNSG
//
