ID A0A0A3W694_9GAMM Unreviewed; 894 AA.
AC A0A0A3W694;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=GW12_14480 {ECO:0000313|EMBL:KGT47536.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT47536.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT47536.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT47536.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) 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:KGT47536.1}.
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; JPQO01000157; KGT47536.1; -; Genomic_DNA.
DR RefSeq; WP_034585705.1; NZ_JPQO01000157.1.
DR AlphaFoldDB; A0A0A3W694; -.
DR STRING; 1509403.GW12_14480; -.
DR PATRIC; fig|1509403.3.peg.1432; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000032870; Unassembled WGS sequence.
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:KGT47536.1}.
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; 102063 MW; 6CAEE014C9E9D821 CRC64;
MAQQIDAPLR DDVRLLGNLL GETLKLHAGQ DLFNQVEQIR ALSKGARDGQ VEAEKQLEQL
FLSLEDHEIL PLARAFTHFL NFANIAEQYH VVRRRRQSEF DETAESPNPL VPLFEKFKQK
EISSETLYQQ ICELKIELVL TAHPTEVSRR TLIQKYDGIN NCLSKCDQQK LTPRERQEVL
ADLKQLITSA WQTDEIRQHR PTPVDEAKWG FTTIEQTLWN AVPKFIRELN EMVQDQCGQP
LPLSVAPVRF ASWMGGDRDG NPNVTHHVTQ KVLWLSRWKA ADLYLRDIED LRWELSIQQC
SEELQQALGK SHPEPYREYL RDTRERLKAT RNWLAEKLHG KDADDSRVIK TKDELLQPLL
LCYRSLMDCN LPEIANGKLL DFIYRVNSFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
FETWTEQARQ NFLLQELQSK RPLLPKYLNE PAGSLIEHPD VQEVFATMRT LAQQPSESLG
AYIISMAEYP SDVLAVLLLQ KEAGIKHPLR VVPLFETLKD LDGAADTMST LFNMHWYKQH
IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKQ HDVKLTLFHG RGGSISRGGA
PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLETIALQN LEIYTAATLE ATLLPPPNPK
PEWRELMHKM TDLSVNVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
SLRAIPWVFA WTQIRLMLPA WLGTGAALNE VLEQGQRPTL DEMLAQWPYF QTLIDMLEMV
LSKADADVAL YYESHLTDDP DLKLLGEELR QRLKDGVQTL LTLKGESKLL TSNDVLDQSM
RVRKPYLLPL HLLQAELMKR RRLYLAQQNA ENTPVDHALM VSIAGIAAGL RNTG
//
