ID   A0A145WHX7_9GAMM        Unreviewed;       896 AA.
AC   A0A145WHX7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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=AMD27_00225 {ECO:0000313|EMBL:AMW77486.1};
OS   Acinetobacter sp. TGL-Y2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77486.1, ECO:0000313|Proteomes:UP000076238};
RN   [1] {ECO:0000313|Proteomes:UP000076238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA   Zhang G.;
RL   Submitted (APR-2016) 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; CP015110; AMW77486.1; -; Genomic_DNA.
DR   RefSeq; WP_067654741.1; NZ_CP015110.1.
DR   AlphaFoldDB; A0A145WHX7; -.
DR   STRING; 1407071.AMD27_00225; -.
DR   KEGG; acv:AMD27_00225; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000076238; 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:AMW77486.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076238}.
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;  102449 MW;  81B112AB322B5560 CRC64;
     MIQHIDAPLR EDVRLLGNLL GETLKEQAGQ DLFNQIEQIR ALSKGARDGN IEAEKQLEQL
     FLTLEDDEIL PLTRAFSHFL NFTNIAEQYH VVRSRRQNEC DEDAASPNVL DPLFDKFKQQ
     QISADVLYQQ ICELNIELVL TAHPTEVSRR TLIQKYDGIN DCLSQFDQQK LTPKQRARVL
     ENLKQLVCSA WQTDEIRQHR PTPIDEAKWG FTTIEQTLWN AIPKFIRELG DLVNAHCERT
     LPLDIAPVRF ASWMGGDRDG NPNVTHKVTQ EVLWLSRWKA ADLYLRDIED LRWELSIQAC
     SDELKNAIGY AHAEPYREYL RSTRERLKIT REWLAAKLQG QHSDVDRSQI IHHKDELLQP
     LLLCYRSLMD CNLAEIANGK LLDFIYRVNC FGIELLKLDI RQESGRHRQA ISAITEYLGL
     GNFETWTEQA RQNFLLQELQ SKRPLLPKHL HVPAQSLIEH PDVQEVFATM RTLAEQPKES
     LGAYIISMAE YPSDVLAVLL LQKEAGIEHP LRVVPLFETL KDLDGAADTM NTLFNMHWYK
     QHIQSKHEVM IGYSDSAKDA GFMSANWAQY RAQEELTSIA KNHDVQLTLF HGRGGSISRG
     GAPTQQALFS QPPGSISGAI RVTEQGEMIR FKFGLEEIAL QNLEIYTAAT LEATLLPPPE
     PKPEWRELMH KMTDLSVQVY RQTVRDNPHF VQYLRTVTPE LELQMLPLGS RPAKRKVSGG
     IESLRAIPWV FAWTQIRLML PAWLGTGAAI NQVITQGHKP ELDEMLQQWP YFQTLIDMLE
     MVLSKADSNI ALYYESHLTD DENLKVLGAE LRTRLHDAVQ TLLAMKGESK LLSSNDVLDQ
     SMKVRKPYLL PLHLLQAELM KRRREYLSHQ SAEQTPVDHA LMVSIAGIAA GLRNTG
//