CAPP_STRMU
ID CAPP_STRMU Reviewed; 907 AA.
AC Q8DV10;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; Synonyms=capP;
GN OrderedLocusNames=SMU_712;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC 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; AE014133; AAN58441.1; -; Genomic_DNA.
DR RefSeq; NP_721135.1; NC_004350.2.
DR RefSeq; WP_002263316.1; NC_004350.2.
DR AlphaFoldDB; Q8DV10; -.
DR SMR; Q8DV10; -.
DR STRING; 210007.SMU_712; -.
DR PRIDE; Q8DV10; -.
DR EnsemblBacteria; AAN58441; AAN58441; SMU_712.
DR KEGG; smu:SMU_712; -.
DR PATRIC; fig|210007.7.peg.631; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
DR PhylomeDB; Q8DV10; -.
DR Proteomes; UP000002512; 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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT CHAIN 1..907
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166629"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 570
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 907 AA; 103896 MW; 286DAB90F19FBE8C CRC64;
MTINKLESRN DKEAIAEEIT ILTKLLDDAT KTMVGSASFD KITLFKKLSI EEKHQELERE
IEQLTNEEMV VVSRYFSILP LLINISEDVN LAYEINYQNN NDIDYLGKLS ATIELVSSQK
NAQEILENVN VVPVLTAHPT QVQRKTMLDL TNHIHELLRK YRDVKAGSIN KQKWYDDMRR
YVELIMQTDI IREKKLKVTN EITNVMEYYN SSLIKGVTKL ITEYKHLSHQ KGFDLGNAKP
ITMGMWIGGD RDGNPFVTAE TLKISALVQN EVILNYYIDK VSDLYRTFSL STSLSTISNA
VKEMADRSTD VSIYREKEPY RKAFHYIQSR LQETLIYLKN NHLEELESED SAQILPYQSA
QEFRNDLQLI KDSLLENNGS AFITGDLTEL LQAVDVFGFF LASIDMRQDS SVHETCVAEL
LASANIVANY SDLPEEEKIA ILLKELTEDP RILSATHVEK SEILQKELAI FKTARKLKDA
LGEDVIKQHI ISHTESISDM FELAIMLKEV GLVDTDKARV QIVPLFETIE DLDNSREIMR
QYLNYDIVKK WIAANHNYQE IMLGYSDSNK DGGYLSSGWA LYKAQNELTE IGYDNGVKIT
FFHGRGGTVG RGGGPSYEAI TSQPFGSIKD RIRLTEQGEV IGNKYGNKDV AYYNLEMLVS
ATLDRMVTRR IVNSDNLVNY RLIMDEIVAD SNLIYRDLVF GNEHFYDYFF AASPIREVSS
LNIGSRPAAR KTITEISGLR AIPWVFSWSQ NRIMFPGWYG VGSAFKHFID KDEKNLTKLQ
EMYQSWPFFH SLLSNVDMVL SKSNMNIAFE YAKLCQDEET KEVFATILDE WQLTKNVILA
IESHKQLLED NSYLKASLDY RLPYFNVLNY IQIELIKRQR RGELGENLEN LIHITINGVA
TGLRNSG