CAPP_STRR6
ID CAPP_STRR6 Reviewed; 898 AA.
AC Q8DPW5;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
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}; OrderedLocusNames=spr0974;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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}.
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DR EMBL; AE007317; AAK99778.1; -; Genomic_DNA.
DR PIR; F97993; F97993.
DR RefSeq; NP_358568.1; NC_003098.1.
DR RefSeq; WP_000058147.1; NC_003098.1.
DR AlphaFoldDB; Q8DPW5; -.
DR SMR; Q8DPW5; -.
DR STRING; 171101.spr0974; -.
DR EnsemblBacteria; AAK99778; AAK99778; spr0974.
DR GeneID; 60232607; -.
DR KEGG; spr:spr0974; -.
DR PATRIC; fig|171101.6.peg.1060; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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..898
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166631"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 561
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 898 AA; 103209 MW; DCDBCE2630E90ED0 CRC64;
MSLQKLENSS NKSVVQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST QEDYQGLNRL
VTSLSNDEMV YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS TTIKLVAEKE
NAVEILEHLN VVPVLTAHPT QVQRKSMLDL TNHIHSLLRK YRDVKLGLIN KDKWYNDLRR
YIEIIMQTDM IREKKLKVTN EITNAMEYYN SSFLKAVPHL TTEYKRLAQA HGLNLKQAKP
ITMGMWIGGD RDGNPFVTAK TLKQSALTQC EVIMNYYDKK IYQLYREFSL STSIVNVSKQ
VREMARQSKD NSIYREKELY RRALFDIQSK IQATKTYLIE DEEVGTRYET ANDFYKDLIA
IRDSLLENKG ESLISGDFVE LLQAVEIFGF YLASIDMRQD SSVYEACVAE LLKSAGIHSR
YSELSEEEKC DLLLKELEED PRILSATHAE KSELLAKELA IFKTARVLKD KLGDDVIRQT
IISHATSLSD MLELAILLKE VGLVDTERAR VQIVPLFETI EDLDHSEETM RKYLSLSLAK
KWIDSRNNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKV TFFHGRGGTV
GRGGGPTYEA ITSQPLKSIK DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SAAINRMITQ
KKSDTNTPNR YEAIMDQVVD RSYDIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI NKNPENIAIL RDMYQNWPFF
QSLLSNVDMV LSKSNMNIAF EYAKLCEDEQ VKAIYETILN EWQVTKNVIL AIEGHDELLA
DNPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE RLIHITINGI ATGLRNSG