ID N9C8N8_9GAMM Unreviewed; 894 AA.
AC N9C8N8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=F941_02704 {ECO:0000313|EMBL:ENV81886.1};
OS Acinetobacter bouvetii DSM 14964 = CIP 107468.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120925 {ECO:0000313|EMBL:ENV81886.1, ECO:0000313|Proteomes:UP000018460};
RN [1] {ECO:0000313|EMBL:ENV81886.1, ECO:0000313|Proteomes:UP000018460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107468 {ECO:0000313|EMBL:ENV81886.1,
RC ECO:0000313|Proteomes:UP000018460};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter bouvetii CIP 107468.";
RL Submitted (FEB-2013) 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:ENV81886.1}.
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DR EMBL; APQD01000020; ENV81886.1; -; Genomic_DNA.
DR RefSeq; WP_005012310.1; NZ_KB892278.1.
DR AlphaFoldDB; N9C8N8; -.
DR PATRIC; fig|1120925.3.peg.2848; -.
DR eggNOG; COG2352; Bacteria.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000018460; 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:ENV81886.1}.
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; 102038 MW; A929BA5F0B814C6E CRC64;
MIQQIDAPLR DDVRLLGNLL GETLKQHAGQ DLFNQVEQIR ALAKGARDGQ AEAEKQLEQL
FLSLEDDEIL PLTRAFTHFL NFANIAEQYH VVRSRRQSEF DEQAPSPNPL DHLFQKFKDR
DISAEALYQQ ICELKIELVL TAHPTEVSRR TLIQKYDGIN DCLFKFDQQK LTPRERQAVL
DDLKQLVCSA WQTDEIRQHR PTPVDEAKWG FTTIEQTLWN AVPKFMRELD SMVTEHCGQQ
LPLTIAPVRF ASWMGGDRDG NPNVTHNITQ EVLWLSRWKA ADLYVRDIEA LRWELSIEQC
SAELRAALGQ DHPEPYREYL RDTRQRLKAT RYWLAQKLKG EDADDSQVIR SKDELLQPLL
LCYRSLIDCD LPEIANGKLL DFIHRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
FETWTEQARQ NFLLQELQSK RPLLPKHLNE PEQSLIEHPD VQEVFATMRT LAEQPSESLG
AYIISMAEYP SDVLAVLLLQ KEAGIQQALR VVPLFETLKD LDGAAATMQT LFGMHWYKQH
IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTEIAKK HGVQLTLFHG RGGSISRGGA
PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIALQN LEIYTAATLE ATLLPPPEPK
QEWRALMHKM TELSVQVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
SLRAIPWVFA WTQIRLMLPA WLGTGAAINQ VLDQGQKAVL EEMLHEWPYF QTLIDMLEMV
LSKSDSHVAL YYESHLTQDE DLKALGEELR QRLRDAVQTL LALKGESKLL SSNDVLDQSM
KVRKPYLLPL HLLQAELMKR RRAYLAERQA ENTPVDHALM VSIAGIAAGL RNTG
//
