ID   Q1JHV9_STRPD            Unreviewed;       937 AA.
AC   Q1JHV9;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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:ABF33564.1};
GN   OrderedLocusNames=MGAS10270_Spy0499 {ECO:0000313|EMBL:ABF33564.1};
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552 {ECO:0000313|EMBL:ABF33564.1, ECO:0000313|Proteomes:UP000002436};
RN   [1] {ECO:0000313|EMBL:ABF33564.1, ECO:0000313|Proteomes:UP000002436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10270 {ECO:0000313|EMBL:ABF33564.1,
RC   ECO:0000313|Proteomes:UP000002436};
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF33564.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1JHV9; -.
DR   KEGG; sph:MGAS10270_Spy0499; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002436; 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:ABF33564.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        600
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   937 AA;  106395 MW;  90025C0F2F3BC24A CRC64;
     MVKSGMIEET SKEGDGHLPL KKLESSNNQA IIAEEVALLK EMLENITRRM IGDDAFTVIE
     SIVVLSEKQD YIELEKVVAN ISNQEMEVIS RYFSILPLLI NISEDVDLAY EINHQNNTDT
     DYLGKLALTI KDLAGKDNGK DILEQVNVVP VLTAHPTQVQ RKTILELTTH IHKLLRKYRD
     AKAGVINLEK WRQELYRYIE MIMQTDIIRE KKLQVKNEIK NVMQYYDGSL IQAVTKLTTE
     YKNLAQKHGL ELDNPKPITM GMWIGGDRDG NPFVTAETLC LSATVQSEVI LNYYIDKLAA
     LYRTFSLSST LVQPNSEVER LASLSQDQSI YRGNEPYRRA FHYIQSRLKQ TQIQLTNQPA
     ARMSSSVGLS TSAWSSPASL ENPILAYDSP VDFKADLKAI EQSLLDNGNS ALIEGDLREV
     MQAVDIFGFF LASIDMRQDS SVQEACVAEL LKGANIVDDY SSLSETEKCD VLVQQLMEEP
     RTLSSAAVAK SDLLEKELAI YTTARELKDK LGEEVIKQHI ISHTESVSDM FELAIMLKEV
     GLVDQQRARV QIVPLFETIE DLDNARDIMA AYLSHDIVKS WIATNRNYQE IMLGYSDSNK
     DGGYLASGWT LYKAQNELTA IGEEHGVKIT FFHGRGGTVG RGGGPSYDAI TSQPFGSIKD
     RIRLTEQGEI IENKYGNKDV AYYHLEMLIS ASINRMVTQM ITDPNEIDSF REIMDSIVAD
     SNTIYRKLVF DNPHFYDYFF EASPIKEVSS LNIGSRPAAR KTITEITGLR AIPWVFSWSQ
     NRIMFPGWYG VGSAFKRYID RAQGNLERLQ HMYQTWPFFH SLLSNVDMVL SKSNMNIAFQ
     YAQLAESQDV RDVFYEILDE WQLTKNVILA IQDHDDLLED NPSLKHSLKS RLPYFNVLNY
     IQIELIKRWR NNQLDENDEK LIHTTINGIA TGLRNSG
//