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}.
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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
//