ID A0A139P7S9_9STRE Unreviewed; 948 AA.
AC A0A139P7S9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=STRDD11_01027 {ECO:0000313|EMBL:KXT84346.1};
OS Streptococcus sp. DD11.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT84346.1, ECO:0000313|Proteomes:UP000070514};
RN [1] {ECO:0000313|EMBL:KXT84346.1, ECO:0000313|Proteomes:UP000070514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD11 {ECO:0000313|EMBL:KXT84346.1,
RC ECO:0000313|Proteomes:UP000070514};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) 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,
CC ECO:0000256|HAMAP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT84346.1}.
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; LQRF01000110; KXT84346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139P7S9; -.
DR STRING; 1777879.STRDD11_01027; -.
DR PATRIC; fig|1777879.3.peg.1140; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000070514; Unassembled WGS sequence.
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:KXT84346.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 610
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 948 AA; 108435 MW; 1F30AFA56E764191 CRC64;
MSFKKLESYS NKEVIREEVA ILTDLLSDIT RNILSPETFE KISVMEELAM ASNYQELKAI
VEELTTDEMV YISRYFSILP LLINISEDVD LAYEINHQNN INRDYLGKLS TTIDLISTRE
NAQDILEHLN VVPVLTAHPT QVQRKTMLDL TNHIHSLLRQ HRDVKAGLVN EKKWLANLRR
YIELMMQTDM IREKKLKVTN EITNVMEYYN SSFLQAITNF MVEYRRLAEE KGIQLENPKP
ITMGMWIGGD RDGNPFVTAE TLKLSATVQS EVILNYYIDK VYTLYRTFSL STNLSETSQA
VAELAARSSD TSVYRENEPY RRAFHYIQSK LIQTLLYLKE GDFSGSGRHK AGGPGADRDS
QNSLAVSNKG KEIIPNYIQS RINETLTELK KEDTPSYKTA QEFKDDLLII RDSLIEHHGE
ALVTGDLTEL LQAVDIFGFY LASIDMRQDS SVHEACVAEL LASANIVKDY SSLPEEEKCQ
ILLQQLLEDP RILSATHVPK SDLLQKELEI FRTARQLKDA IGEEVIKQNI ISHSTSVSDL
LELAILLKEV GLIDENGARV QIVPLFETIE DLDNSCDTME KYLSLPIAQK WIASKDNYQE
IMLGYSDSNK DGGYLSSCWT LYKAQQQLTA IGDKFGVKIT FFHGRGGTVG RGGGPTYEAI
TSQPLRSIND RIRLTEQGEV IGNKYGNKDA AYYNLEMLVS AAINRMVTHK KSDTHTSNEY
ERIMDQVVGR SYQIYRDLVF GDERFYDYFF ESSPIKAISS FNIGSRPAAR KTITEIGGLR
AIPWVFSWSQ SRVMFPGWYG VGSSFKEFID EDPEKNLAFL QFMYKRWPFF QSLLSNVDMV
LSKSNMNIAF EYAQLCEDKD VQDIFTIILD EWQLTKNVIL EIEGHEELLA ENTYLKDSLD
YRMPYFNVLN YIQLELIKRQ RRGELSPEQE RLIHITINGI ATGLRNSG
//
