ID   Q31FG0_HYDCU            Unreviewed;       929 AA.
AC   Q31FG0;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=Tcr_1521 {ECO:0000313|EMBL:ABB42113.1};
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB42113.1};
RN   [1] {ECO:0000313|EMBL:ABB42113.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XCL-2 {ECO:0000313|EMBL:ABB42113.1};
RG   US DOE Joint Genome Institute;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA   Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA   Richardson P.;
RT   "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL   Submitted (JUL-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; CP000109; ABB42113.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31FG0; -.
DR   STRING; 317025.Tcr_1521; -.
DR   KEGG; tcx:Tcr_1521; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
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:SF46; 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:ABB42113.1}.
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        588
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   929 AA;  106665 MW;  7271412DE674F80D CRC64;
     MAKELRDKQL RSRVKLLGSL LGEVIETQVG KTTLDAVEKL RKGYIQLHEK ENPELRKELK
     AFIEAQTPDN LILIIRAFNL YFSLVNLAEE EHQFHERQSQ LKSDGPLWMG SVLNTISEFK
     QEGLLAAEVE KLINKLCYIP VFTAHPTESK RRAVMENLRR IFLTLGELNE AEAYNNPYAQ
     EEVIKKLQYQ IQVLWKTDEV RRMKPTVEDE IRNGIYYFRQ SLFKAVPTVY RYMERALARH
     YPEDNIQTPN FLNFGSWIGG DRDGNPFVTH ETTINALLMQ SRAAIYEYQK RVYELSSHLT
     QSRYISEIKQ EVINRATIID ADLQERVFHK RSERFRDEPY RRFLYLIHGR LQENLNYIEA
     QLNAETAEKP KFGYNSEQEF LDDLELIYDS LCSHGDQEVA DANLKDLIRL VQTFGFYLMR
     LDIRQESTVH TDAVADLLSH LGIDYLSLSE AERLDLLAQQ VSSPTVIDTQ HLDLKEMTLE
     VLEVFNVMRR MREEISEKAF NNYVISMTHE ASHVMEVLFL AHQAGLAGYN AGEPYCKIRV
     SPLFETIQDL EHIVPVTSAL FDNPTYHALL KASGNQQEIM LGYSDSAKDG GNLSSAWTLY
     QAQQQIMKLA DEYKIDCRLF HGRGGTVGRG GGPTHSAILS QPTGTVRGEI KFTEQGEVLS
     YKYSNAETAM YELSMGITGL MKASKCLVKP AQQDNPQHLE AMQKLAKEGE HAFRELTDHT
     EGFFKFFYEA TPVNEIGLLN IGSRPSHRKK GNLSKSSIRA IPWIFGWAQA RLTFPAWYGT
     GSALHNWMKT QTPEQLKEMY ENWPFFKGLL SNIQMALFKT DLIIGKDYSE LGQDQKQAQH
     IYNMIAEEHV RSVETCLEIS GNEYLMADTP QVALSLARRT PYLEPLNHIQ VAVLKRYKDE
     TLSDEEREEW LTPLLNSINA IAAGMRNTG
//