ID A0A0M5JL68_9GAMM Unreviewed; 894 AA.
AC A0A0M5JL68;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AMQ28_07875 {ECO:0000313|EMBL:ALD02282.1};
OS Acinetobacter sp. TTH0-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD02282.1, ECO:0000313|Proteomes:UP000055186};
RN [1] {ECO:0000313|EMBL:ALD02282.1, ECO:0000313|Proteomes:UP000055186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD02282.1,
RC ECO:0000313|Proteomes:UP000055186};
RA Zhang G.;
RT "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT permafrost region.";
RL Submitted (SEP-2015) 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; CP012608; ALD02282.1; -; Genomic_DNA.
DR RefSeq; WP_053579127.1; NZ_CP012608.1.
DR AlphaFoldDB; A0A0M5JL68; -.
DR STRING; 1646498.AMQ28_07875; -.
DR KEGG; att:AMQ28_07875; -.
DR PATRIC; fig|1646498.3.peg.1595; -.
DR Proteomes; UP000055186; 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:ALD02282.1}.
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; 102106 MW; E2A3682D45E73EE3 CRC64;
MIQQIDAPLR EDVRLLGNLL GETLKEHAGQ DLFNQVEQIR ALSKGARDGQ IEAEKQLEQL
FLTLEDDEIL PLTRAFTHFL NFANIAEQYN VVRSRRKSEF DGQGPSPNPL DHLFQKFKDH
DISANTLFHQ ICELNIELVL TAHPTEVSRR TLIQKYDDIN DCLFKADQQK LTPRERKTIL
QELKQLVCSA WQTDEIRQHR PTPVDEAKWG FTTIEQTLWN AVPKFIRELN EMVEDHCGQR
LPLNIAPVRF ASWMGGDRDG NPNVTHSITQ EVLWLSRWKA ADLYLRDIED LRWELSIQNC
SQELTDALGH AHAEPYREYL RDTRERLKAT RHWLTQKLQG LDADDSAVIK SKDELLQPLL
LCYRSLIACH LTDIANGKLL DFIHRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
FETWTEQARQ NFLLQELQSK RPLLPKHLSE PKQSLIEHPD VQEVFATMRT LAEQPKESLG
AYIISMAEYP SDVLAVLLLQ KEAGIQHALR VVPLFETLKD LDGAADAMNT LFNMHWYKQH
IQAKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKK HAVQLTLFHG RGGSISRGGA
PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIALQN LEIYTAATLE ATLLPPPVPK
DEWRQLMHSM TDLSVQVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
SLRAIPWVFA WTQIRLMLPA WLGTGAAINQ MLDQGQKPLL DEMLQQWPYF QTLIDMLEMV
LSKSDSHVAL YYESHLTDDE DLKILGEQLR QRLKDAVQTL LALKGESQLL SSNEVLDQSM
KVRKPYLLPL HLLQAELMKR RRRYLAECQA EHTPVDHALM VSIAGIAAGL RNTG
//
