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Database: UniProt/TrEMBL
Entry: B2FPC5_STRMK
LinkDB: B2FPC5_STRMK
Original site: B2FPC5_STRMK 
ID   B2FPC5_STRMK            Unreviewed;       903 AA.
AC   B2FPC5;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 92.
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:CAQ44354.1};
GN   OrderedLocusNames=Smlt0778 {ECO:0000313|EMBL:CAQ44354.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44354.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ44354.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ44354.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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}.
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DR   EMBL; AM743169; CAQ44354.1; -; Genomic_DNA.
DR   RefSeq; WP_012479170.1; NC_010943.1.
DR   AlphaFoldDB; B2FPC5; -.
DR   EnsemblBacteria; CAQ44354; CAQ44354; Smlt0778.
DR   KEGG; sml:Smlt0778; -.
DR   PATRIC; fig|522373.3.peg.743; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008840; 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   Reference proteome {ECO:0000313|Proteomes:UP000008840}.
FT   ACT_SITE        151
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        569
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   903 AA;  99657 MW;  3159C78F206EDC22 CRC64;
     MNEYRSSIEF ASPDLPLRDD VRRLGALVGD LLVEQVSAAF LDDVEDVRTR AIARRENQAP
     LSELADGLAG RTPQQAETMV RAFSTYFQVV NIAERVHRIR RRRDYQRAGT AGAQPDGLQD
     ALQHLKAQGV GLDELAQWLP RIDIEPVFTA HPTEAVRRAL LEKEQLMVAS LVDNLDGQRT
     PGEAAADAAR FRMALTASWQ TTDSSPVRPT VDDEREHVGF YLVQVLYRVI PVLYESLQQA
     LRDTYGEELP LPRLLRFGTW VGGDMDGNPN VDAHTIRNTL DAQRQAVLGR YQKELLQLAS
     LLSQSTERVG VSDALQARVA QYQQLLPQVQ SRPRHADMPY RLLNDRMRAR LQATLDNGGG
     AYAGPAELID DLQLILDSLL ANRGEHAGGF AVQRLLWRVK TFGFHLARLD VRQESSVHAR
     ALAAVLGGEE AWQALDVAGR ARLLSPHASG ETALPNGDDE GNQRLDAVFA ALADARARHG
     SDALGSYIIS MAHDRSDVLA VLALARRGGL VEENGSVPLD IAPLFETVDD LKRGTATLRD
     LLADPIYRAH LQARDDVQMV MLGYSDSSKD GGIAASRWGL QRAQVELLEV AAEAGIRLTF
     FHGRGGSISR GGGKTTHAVD ASPRGSIDGR LRVTEQGEVI HRKYGIRALA LRSLEQATGA
     VLRASLRPRA AEPREDDWRP VMDAVAGASS EVYRAFVGQA GFMDYFRTAT PIDVIERMTL
     GSRPSRRLGQ DAALGNLRAI PWVFAWSQAR AVIPGWYGVG SGLQAAVDAG HEQTLRDMAR
     DWPFFRTFLD DISMVLSKGD ITIAEQFSQL SGELHGRFFP QVQRELELTR HWLLALMDQQ
     TLLDHDARLA LSIRLRNPYV DPISMLQVDL LQRWRASGRE DDDLLRALVA CVNGVSQGVQ
     NTG
//
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