GenomeNet

Database: UniProt
Entry: I4ZQ48_9GAMM
LinkDB: I4ZQ48_9GAMM
Original site: I4ZQ48_9GAMM 
ID   I4ZQ48_9GAMM            Unreviewed;       894 AA.
AC   I4ZQ48;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=HADU_12879 {ECO:0000313|EMBL:EIM38340.1}, HADU_13363
GN   {ECO:0000313|EMBL:EIM38166.1};
OS   Acinetobacter sp. HA.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM38340.1, ECO:0000313|Proteomes:UP000018434};
RN   [1] {ECO:0000313|EMBL:EIM38340.1, ECO:0000313|Proteomes:UP000018434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA {ECO:0000313|EMBL:EIM38340.1,
RC   ECO:0000313|Proteomes:UP000018434};
RX   PubMed=22933775; DOI=10.1128/JB.01194-12;
RA   Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA   Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT   "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT   the Polyphagous Insect Pest Helicoverpa armigera.";
RL   J. Bacteriol. 194:5156-5156(2012).
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:EIM38340.1}.
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; AJXD01000096; EIM38166.1; -; Genomic_DNA.
DR   EMBL; AJXD01000095; EIM38340.1; -; Genomic_DNA.
DR   RefSeq; WP_008306988.1; NZ_AJXD01000096.1.
DR   AlphaFoldDB; I4ZQ48; -.
DR   PATRIC; fig|1173062.3.peg.2506; -.
DR   Proteomes; UP000018434; 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:EIM38340.1}.
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;  101777 MW;  9026D266553AB29B CRC64;
     MAQQIDAPLR EDVRLLGNLL GETLKLHAGQ DLFNQVEQIR ALSKGARDGQ LEAEKQLEQL
     FLSLEDDEIL PLTRAFTHFL NFANIAEQYH VVRRRRQSEF DETAESPNPL VPLFEKFKQQ
     EISAESLYQQ ICELKIELVL TAHPTEVSRR TLIQKYDGIN DCLSKCDQQK LTPRERQAIL
     AELKQLITSA WQTDEIRQHR PTPVDEAKWG FTTIEQTLWN AVPKFIRELD GMVQEQCGQS
     LPLSVAPVRF ASWMGGDRDG NPNVTHHITQ EVLWLSRWKA ADLYLRDIED LRWELSIQQC
     SEELQQALGS SHPEPYREYL RDTRERLKAT RHWLAEKLHG HDADDSQVIK TKDELLQPLL
     LCYRSLLACN LPEIANGKLL DFIYRVNSFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
     FETWTEQARQ NFLLQELQSK RPLLPKYLNE PAGSLIEHPD VQEVFATMRT LAEQPSESLG
     AYIISMAEYP SDVLAVLLLQ KEAGIKQALR VVPLFETLKD LDDAASTMST LFNMHWYKQH
     IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKQ HGIQLTLFHG RGGSISRGGA
     PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIALQN LEIYTAATLE ATLLPPPVPK
     TEWRDLMHQM TDLSVQVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
     SLRAIPWVFA WTQIRLMLPA WLGTGAALNE VLDQGQRATL DEMLAQWPYF QTLIDMLEMV
     LSKADGDVAL YYESHLTHDP DLKVLGEELR QRLKDAVQTL LTLKGESKLL TSNDVLDQSM
     RVRKPYLLPL HLLQAELMKR RRLYLAEQNA EHTPVDHALM VSIAGIAAGL RNTG
//
DBGET integrated database retrieval system