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
//