ID A0A139NKJ5_9STRE Unreviewed; 915 AA.
AC A0A139NKJ5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=STRDD12_00556 {ECO:0000313|EMBL:KXT76377.1};
OS Streptococcus sp. DD12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT76377.1, ECO:0000313|Proteomes:UP000070638};
RN [1] {ECO:0000313|EMBL:KXT76377.1, ECO:0000313|Proteomes:UP000070638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD12 {ECO:0000313|EMBL:KXT76377.1,
RC ECO:0000313|Proteomes:UP000070638};
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:KXT76377.1}.
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DR EMBL; LQRG01000007; KXT76377.1; -; Genomic_DNA.
DR RefSeq; WP_066914948.1; NZ_KQ969495.1.
DR AlphaFoldDB; A0A139NKJ5; -.
DR STRING; 1777880.STRDD12_00556; -.
DR PATRIC; fig|1777880.3.peg.576; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000070638; 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:KXT76377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070638}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 578
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 915 AA; 104113 MW; 91E0092126AA9563 CRC64;
MATKRLENNT NADIVREEIA ILTQLLDETT QKLIGPSGLA HIKEMTRLSA KGDYQALENL
ISQMDNQEMV VVSRYFAILP LLINISEDVD LAYEINYENN VGQDYLGKLE HTIDLVTEHK
NAQEILEHVN VVPVLTAHPT QVQRKTMLEL NNQIHELLRK HRDVKEGRIN KEKWESDLKR
YVETMMQSDI IREKKLKVTN EISNVMEYYN SSLIPAITKL TSRYQKLAAQ KGLSLDDSKP
ITMGMWIGGD RDGNPYVTAE TLRLSAMVQN EVIMNYYLDK LSALYRTFSL SDNLIQVTEA
LRALADKSSD TSEFREKEPY RRAFNYIQHK ISQTLAHIQG RQEQAQSLPT WATESAAVTE
ELDVYANVSE FQADLAVIKD SLVSNGDEDL IDGEFEELLE AARVFGFFLA TIDMRQDSSV
HEACVDELLR EANIVPNYSD LSETEKVAVL LKELQEDPRT LSSANADKSE LLQKELAIFQ
TARDLKDTLG EDVIKQHIIS HSESVSDLFE LAILLKEVGL LDTDKARIMV APLFETIEDL
ENSGDIMRQY LSYDIVKRWI AQNKGYQEIM LGYSDSNKDG GYLSSGWTLY KAQNELTQIG
EERGIKITFF HGRGGTVGRG GGPSYEAITS QPFGTIKDRI RLTEQGEVIG YKYGNKDAAY
YNLEMLVSAA IDRMATGMIT SSEEIGDYRE AMESIVTDSY QIYRDLVFGN PHFYDYFFEA
SPIKEVSSLN IGSRPAARKT ITEISGLRAI PWVFSWSQNR IMFPGWYGVG SAFKHFIDQA
EGNLERLQHM YKTWPFFNSL LSNVDMVLSK SNMNIAFQYA QLAKDPAVRE VFNIILDEWQ
LTKDVILAIE QQEDFIEESP SLKASLEYRL PYFNVLNYVQ IELIKRLRKG ELDEETEKLI
HITINGIATG LRNSG
//
