ID   F6D980_THICA            Unreviewed;       935 AA.
AC   F6D980;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=Thicy_1240 {ECO:0000313|EMBL:AEG32007.1};
OS   Thiomicrospira cyclica (strain DSM 14477 / JCM 11371 / ALM1)
OS   (Thioalkalimicrobium cyclicum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=717773 {ECO:0000313|EMBL:AEG32007.1, ECO:0000313|Proteomes:UP000009232};
RN   [1] {ECO:0000313|EMBL:AEG32007.1, ECO:0000313|Proteomes:UP000009232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14477 / JCM 11371 / ALM1
RC   {ECO:0000313|Proteomes:UP000009232};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.;
RT   "Complete sequence of Thioalkalimicrobium cyclicum ALM1.";
RL   Submitted (MAY-2011) 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; CP002776; AEG32007.1; -; Genomic_DNA.
DR   RefSeq; WP_013835783.1; NC_015581.1.
DR   AlphaFoldDB; F6D980; -.
DR   STRING; 717773.Thicy_1240; -.
DR   KEGG; tcy:Thicy_1240; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009232; 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: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:AEG32007.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009232}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   935 AA;  106603 MW;  3FEA497D49476F1F CRC64;
     MNVSAQTESH DKQLRARVKL LGQLLGEVIE SQVGRTTLDA VEKLRRGYIQ LRKQDDPELR
     QSLVTFIEQQ SPENLILIIR AFNIYFSLAN LAEEEHQYHG RQSQLKSDGP LWMGSMLQTI
     GEFKEAGLAS EDVSKLLSKI KYIPVFTAHP TESKRRAVME NLRRIFVTLD GLNEAETHNN
     SYTRQDVISK LRYQIQVLWK TDEVRQTKPT VSDEIRNGIY YFRQSLFQSV PQVYRYLERA
     LGRHYPDIAH QVPPFLTFGS WIGGDRDGNP FVTHQTTREA IYLQSRSVLY EYEKRLLELS
     AMLTHSRHIC DIHQDIINRA TIVDADLLEK VFHKRAERFK DEPYRRFLYL MRGRIRENLA
     YIEARLNNEQ PPQSSSRFAY SSEDEFLADL QLIHESLCNH GDQSVANATL KDLIRLVETF
     GFYLMRLDIR QESTVHTEAV AELLSHLEID YNQLDEADKL NLLAKHVASA TIIDTQHLAL
     KPMTAEVLEV FNALRELRKE ISPKAFNNYV ISMTHEASHV MEVLFLAHQA GLAGYNAGEP
     YCDIHITPLF ETIEDLGHIV PVTENLFNNP TYLALLKASG NQQEIMLGYS DSAKDGGNLS
     SAWSLYQAQQ KIMKVADAFE IDCRLFHGRG GTIGRGGGPT HMAILSQPTG TVRGEIKFTE
     QGEVLSYKYS NSETASYELS LGVTGLMKAS LCLVKDVTKD DPTHLSTMEQ LAKDGEASYR
     LLTDHTEGFF KLFYEATPVN EIGLLNIGSR PSHRKKGNLS KSSIRAIPWV FGWAQARLTF
     PAWFGTGHAL DEWTKHNSQA GLLDMYNKWP FFRALLSNIQ MALYKTQLIT GKEYCEIASD
     REQAMHIYNM IAEEHARTVE YSLSVSDNPY LMAETPSIAL SLQRRNPYLD PLNHIQIVLL
     KRFKDESVSE QERDIWLKPL LNSINAIAAG MRNTG
//