ID L9MBT6_9GAMM Unreviewed; 896 AA.
AC L9MBT6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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_1 {ECO:0000313|EMBL:ELW84409.1};
GN Synonyms=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN ORFNames=ACINWC743_0094 {ECO:0000313|EMBL:ELW84409.1};
OS Acinetobacter sp. WC-743.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=903945 {ECO:0000313|EMBL:ELW84409.1, ECO:0000313|Proteomes:UP000011515};
RN [1] {ECO:0000313|EMBL:ELW84409.1, ECO:0000313|Proteomes:UP000011515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WC-743 {ECO:0000313|EMBL:ELW84409.1,
RC ECO:0000313|Proteomes:UP000011515};
RA Harkins D.M., Brinkac L.M., Durkin A.S., Beck E., Fedorova N.B., Kim M.,
RA Onuska J., Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A.,
RA Cash D.M., Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.;
RL Submitted (SEP-2012) 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:ELW84409.1}.
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DR EMBL; AMFQ01000076; ELW84409.1; -; Genomic_DNA.
DR RefSeq; WP_009585371.1; NZ_AMFQ01000076.1.
DR AlphaFoldDB; L9MBT6; -.
DR PATRIC; fig|903945.3.peg.1999; -.
DR Proteomes; UP000011515; 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:ELW84409.1}.
FT ACT_SITE 143
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 558
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 896 AA; 102153 MW; 184F999C11C794DE CRC64;
MVQQIDAPLR EDVRLLGNLL GETLKEHAGQ DLFNQIEQIR ALGKGARDGQ IEAEKQLEQL
FLNLKDYEIL PLTRAFSHFL NFANIAEQYH VVRSRRQSEC DEHAPSPNVL DHLFSKFKDQ
QISAETLYQQ ICELKIELVL TAHPTEVSRR TLIQKYDGIN HCLSTFDQQK LTPKQRAEVL
TDLKQLICSA WQTDEIRQHR PTPIDEAKWG FTTIEQTLWN AVPKFIRELD DLVQGNCAQA
LPLDISPIRF ASWMGGDRDG NPNVTHNITQ EVLWLSRWKA ADLYLRDIED LRWELSIEAY
SNELHQALGY SHPEPYREYL RATRERLKAT RQWLADKLRG QHSDVDRSLI IRHKDELLQP
LLLCYRSLMA CNLPEIANGK LLDFIYRVNC FGIELLKLDI RQESGRHRQA ISAITEYLGL
GNFETWTEQA RQNFLLQELQ SKRPLLPKHL NEPANSLIEH PDVQEVFATM RTLAEQPKES
LGAYIISMAE YPSDVLAVLL LQKEAGIEHP LRVVPLFETL KDLDGAASTM TTLFNMHWYK
QHIQGKHEVM IGYSDSAKDA GFMSANWAQY RAQEELTAIA KQHGIQLTLF HGRGGSISRG
GAPTQQALFS QPPGSISGAI RVTEQGEMIR FKFGLEEIAL QNLEIYAAAT LEATLLPPPV
PKQAWRDLMH NMTDLSVQVY RQTVRENPHF VKYLRTVTPE LELQMLPLGS RPAKRKVSGG
IESLRAIPWV FAWTQIRLML PAWLGTGAAI NQVIDQGQKA VLDEMLSEWP YFQTLIDMLE
MVLSKADSNI ALYYESHLTD DEDLKVLGAE LRQRLHDAVQ TLLAMKGESA LLSSNEVLDQ
AMKVRKPYLL PLHLLQAELM KRRRAYLAEF QAEHTPVDHA LMVSIAGIAA GLRNTG
//
