ID   Q0AC21_ALKEH            Unreviewed;       882 AA.
AC   Q0AC21;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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   OrderedLocusNames=Mlg_0261 {ECO:0000313|EMBL:ABI55616.1};
OS   Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI55616.1, ECO:0000313|Proteomes:UP000001962};
RN   [1] {ECO:0000313|Proteomes:UP000001962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC   {ECO:0000313|Proteomes:UP000001962};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA   Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA   Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) 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, ECO:0000256|HAMAP-
CC         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; CP000453; ABI55616.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0AC21; -.
DR   KEGG; aeh:Mlg_0261; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000001962; 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:ABI55616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001962}.
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        550
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   882 AA;  98934 MW;  50AEBE393F332BD8 CRC64;
     MSIQDSDAAL RDDIRLLGEM LGDTLKEQEG TDLFDTVERI RALAKQARAG DQGAAEALEQ
     ELGSLDEHQI MPVARAFSQF LNLANIAEQH HRVRRSREWA RSPDASPLKG SLAEAFPRLL
     QGETDPEALY HAACELDIEL VLTAHPTETQ RRTMLQKYNR IARLLDGRDR LDLTPDETEE
     VTAGLRREII GAWQSDEIRR RRPTPVDEAR WGLAVMEQVL WDAVPRYLRN LDRSLREHTG
     RALPLDAAPI RFGSWMGGDR DGNPNVTARV TREVCLAGRW MAATLYEKEI QTLINTLSMT
     RCDQALRELV GDAWEPYRVL LKRLRARLRL TQRWVEARLA GKRPPEGEVL LDKEDLLRPL
     LTCYHSLHRC GAGQVAEGEL LDTIRRVSCF GLTLTRLDIR QHADRHADAL SEITSALGLG
     RYDQWDEEAR QRWLLSELAS RRPLIPDDLE PGEEAAEVLE TCRTLAELGS DGLGAYIISM
     AEHPSDILAV ELLQKACGVT QPLRSVPLFE TRDTLQNAAE TMRVLFEQPW YRDRIGGHQE
     IMIGYSDSGK DAGHLTAAWT LYQAQEALVA LAEENGIQLT LFHGRGGSIG RGGGPTHAAV
     LSLPPGSVKG TLRVTEQGEV IQSKFGLPGI ALRNLEIYTA AVLEATLQPP AEPRPEWREV
     MDRLSDTACG AYRGLVKETP EFIEYFQAAT PVREIGQLAI GSRPAKRNQK ALTVDNLRAI
     PWIFAWTQTR LMLPAWLGVG DALSEALEED LGDTLREMFQ QWPFFEAFLD MVEMVLAKGD
     PGVASLYDRR LVPEELHGMG EQLRGRYRKT LDAVLSVTGH ERPLADFPVV RRAVDVRNPY
     VDPLNLLQAE LLYRSRLCDD EQLRRVLMVA INGIAAGMRN TG
//