ID C0DUU2_EIKCO Unreviewed; 902 AA.
AC C0DUU2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
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:EEG24490.1};
GN ORFNames=EIKCOROL_01128 {ECO:0000313|EMBL:EEG24490.1};
OS Eikenella corrodens ATCC 23834.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Eikenella.
OX NCBI_TaxID=546274 {ECO:0000313|EMBL:EEG24490.1, ECO:0000313|Proteomes:UP000005837};
RN [1] {ECO:0000313|EMBL:EEG24490.1, ECO:0000313|Proteomes:UP000005837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23834 {ECO:0000313|EMBL:EEG24490.1,
RC ECO:0000313|Proteomes:UP000005837};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
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:EEG24490.1}.
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DR EMBL; ACEA01000017; EEG24490.1; -; Genomic_DNA.
DR AlphaFoldDB; C0DUU2; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR Proteomes; UP000005837; 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:EEG24490.1};
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:EEG24490.1};
KW Transferase {ECO:0000313|EMBL:EEG24490.1}.
FT ACT_SITE 141
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 569
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 902 AA; 100689 MW; 71321EEF87E87A3D CRC64;
MMPEPSGQHP YKDAPLFDDV AFLTGALQTV LAAQTDCPVQ EAVAALLGGE APQDVVTRSL
PQLNDQQLED LIRACSLFAQ ILNIAEDAHH QRRRLAHSQT RDNAKSTFGH TLDLLQQQGV
SAEALQQQLN HTEVAAVLTA HPTEVQRQTT LTLHRQIRNL LDQRANQAGQ NEERLQQQVQ
TMLWTLWQTN ENRHFKITVA DEISNGIMYF PLSFFSAVPG VYRKLEAALQ VAFPHTRLPN
VLHIGGWIGG DRDGNPFVSA DTLRTAFAQQ ASAVFRFYRS QLYKLYEELP MSIRRVNVSP
EVLALSAKSP DTERAHEEEP YRRALAYILA RTVATAHRFG SGLGSQFGLL EPYDTVEEFL
ADLHIVHTSL CANGSRLLAD GRLADLIRAA SVFRFYLMPL DLRQHAQKHI DVVAELFAAA
GLEDFAALNE AERERVLLRE LSSPRPLHSP FARYSEDTEH ELAIFRAAAE IKAGFGEEAI
RQSIISNAEN VSEMLALALI MKETGLLRLN TEGLPESRLN IVPLFETIEA LQDCIGVMDH
LFSLPWYRHL LADRSNIQEI MLGYSDSNKD GGYVTSQWVL YQAEQALVKL FAKHQVRLRL
FHGRGGSVGR GGGPSYEAVL AQPAGSVAGQ IRITEQGEVI TAKYADADNA ERNLETLVAA
ALEASLLPHR TEEPDAALMQ SLSDAAFAYY RELITHPDFV GYFLQTSPIN EIASLNIGSR
PASRKTLARI QDLRAIPWVF SWTQNRLMLP AWYGFGSAVE QLLRDNPANL EHLRHMVQHS
AFFQAMLSNM EQVMAKADLD IARAYVGLAD QPQAAQAMFE LIAGEFERSR RALLQLIEQD
HLLTDNRSLA RSLALRIPYL NALNWLQVAL LARLRQHPGN PQLIHLIHLT INGVAQGLRN
TG
//
