ID A0A1P8EKY7_9GAMM Unreviewed; 894 AA.
AC A0A1P8EKY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=BEN76_12985 {ECO:0000313|EMBL:APV36881.1};
OS Acinetobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=487316 {ECO:0000313|EMBL:APV36881.1, ECO:0000313|Proteomes:UP000185674};
RN [1] {ECO:0000313|EMBL:APV36881.1, ECO:0000313|Proteomes:UP000185674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFJ2 {ECO:0000313|EMBL:APV36881.1,
RC ECO:0000313|Proteomes:UP000185674};
RA Tabata M., Kuboki S., Gibu N., Kinouchi Y., Vangnai A., Kasai D.,
RA Fukuda M.;
RT "Complete genome sequence of Acinetobacter baylyi strain GFJ2.";
RL Submitted (AUG-2016) 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}.
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DR EMBL; CP016896; APV36881.1; -; Genomic_DNA.
DR RefSeq; WP_076033259.1; NZ_CP016896.1.
DR AlphaFoldDB; A0A1P8EKY7; -.
DR STRING; 487316.BEN76_12985; -.
DR KEGG; asol:BEN76_12985; -.
DR eggNOG; COG2352; Bacteria.
DR Proteomes; UP000185674; 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:APV36881.1}.
FT ACT_SITE 143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 556
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 894 AA; 101985 MW; C1E7211A0CD2219F CRC64;
MIQQIDAPLR EDVRLLGNLL GETLKQHAGQ DLFNQIEQIR ALAKGARDGQ AKVEKQLEKL
FLNLKDEEIL PLTRAFSYFL NFANIAEQYH VVRSRRQSEF DAHAPSPNPL TRLFEKFQHN
HITPQQLFDQ VCELNIELVL TAHPTEVSRR TLIQKYDDIN DALSKLDQQK LTPQEREQVL
TNLKHLICSA WQTDEIRQNK PTPLDEAKWG FTTIEQTLWN AVPKFVRELN TLVHQHCNAT
LPLDISPIRF ASWMGGDRDG NPNVTHTVTQ EVLWLSRWQA ADLYLRDIES LRWELSIQAC
SEELSLALGR SHPEPYREYL RTTRERLKAT RHWLSLRLQG LDGDDSQIIR HKQELLEPLL
LCHRSLIACN LPELANGKLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
FESWTEQARQ NFLIQELQSK RPLLPKYLKE PEGSLIEHPD VKEVFATMRT LAEQPPESLG
AYIISMAEYP SDVLAVLLLQ KEAGILHPLR VVPLFETLKD LDGAAKTMET LFNMDWYKQH
IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKA HNVQLTLFHG RGGSISRGGA
PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGVALQN LEVYTAATLE ATLLPPPVPK
AEWRELMHQM TDISVRVYRE TVRENPHFVQ YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
SLRAIPWVFA WTQIRLMLPA WLGTGAAINQ VIDENKKPLL DEMLAEWPYF QTLIDMLEMV
LSKADANVAL YYESHLTHDD ELKVLGEMLR ARLNDAVQTL LTMKGESKLL SKNDVLDQAM
QVRKPYLLPL HLLQAELMKR RREYTAKTNA DHTPVDHALM VSIAGIAAGL RNTG
//
