ID   B9DRL7_STRU0            Unreviewed;       902 AA.
AC   B9DRL7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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   ECO:0000313|EMBL:CAR41413.1};
GN   OrderedLocusNames=SUB0602 {ECO:0000313|EMBL:CAR41413.1};
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR41413.1, ECO:0000313|Proteomes:UP000000449};
RN   [1] {ECO:0000313|Proteomes:UP000000449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM946015; CAR41413.1; -; Genomic_DNA.
DR   RefSeq; WP_012658125.1; NC_012004.1.
DR   AlphaFoldDB; B9DRL7; -.
DR   STRING; 218495.SUB0602; -.
DR   KEGG; sub:SUB0602; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000449; 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   Reference proteome {ECO:0000313|Proteomes:UP000000449}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   902 AA;  102833 MW;  94905D2B6D0A242C CRC64;
     MAVKKLESSS NQAIIAEEVA ILKTILETIT RDMVGDETFL KIEQIVKLSE QDDYIQLEKM
     IESLTDDEMV IMSRYFSILP LLINISEDVD LAYEINFQNN KGINYLGKLS HTIEEVASKE
     NAKDILENVT VVPVLTAHPT QVQRKTVLEL TNKIHGLLRQ YRDVKSGVIN EEKWLEELRR
     YVEIIMQTDI IREKKLKVKN EITNVMAYYH SSIIPAVTRL TLAYKELAKE KGLELENPKP
     ITMGMWIGGD RDGNPFVTAE TLQLSASIQS QVIIEYYLEK LSKLYRSLSL SSRFSKTSKA
     LDDLAALSSD TSIYREHEPY RKAFHYIQSK MSNTLTSIKE NASHDKQPSD IYETAEDFKK
     DLLIIKDSLV QNGEGTLISG DFSDLLQAVD VFGFFLASID MRQDSSVQEA CVAELLKSAN
     IVDDYSALNE TEKCQILLKE LEEDPRILSA TAVEKSELLE KELAIYKAAR YLKDKLGEDV
     IKQHIISHTE SVSDMFELAI MLKEVGLLDK HMARVQIVPL FETIEDLDNS NAIMTEYLSY
     DIVKNWIASN HNYQEIMLGY SDSNKDGGYL ASGWTLYKAQ NELTEIGSKN GIKITFFHGR
     GGTVGRGGGP SYDAITSQPF GSIKDKIRLT EQGEIIENKF GNKDAAYYNL EMLISASINR
     MVSRMLTNPN EIDGFRETME GIVSYSNKVY RDLVFDNPNF YDYFFEASPI KEVSSLNIGS
     RPAARKTITE ITGLRAIPWV FSWSQNRIMF PGWYGVGSAF KDFIDKEEGN LAKLQHMYKT
     WPFFHSLLSN VDMVLSKSNM NIAYQYAQLA NTQEVKDIYY ILLDEWQLTK NIILAIENHD
     ELLEDHPSLK HSLEFRLPYF NILNYIQIEL IKRLRQNQLG EGYEKLIHTT INGIATGLRN
     SG
//