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Database: UniProt/TrEMBL
Entry: A0A1D8YBR1_9GAMM
LinkDB: A0A1D8YBR1_9GAMM
Original site: A0A1D8YBR1_9GAMM 
ID   A0A1D8YBR1_9GAMM        Unreviewed;       903 AA.
AC   A0A1D8YBR1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-MAR-2018, entry version 9.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=BIZ42_12475 {ECO:0000313|EMBL:AOX62949.1};
OS   Stenotrophomonas sp. LM091.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX62949.1, ECO:0000313|Proteomes:UP000177427};
RN   [1] {ECO:0000313|EMBL:AOX62949.1, ECO:0000313|Proteomes:UP000177427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM091 {ECO:0000313|EMBL:AOX62949.1,
RC   ECO:0000313|Proteomes:UP000177427};
RA   Lefeuvre P.;
RT   "Complete genome sequence of a copper-resistant commensal bacteria:
RT   Stenotrophomonas sp. strain LM091.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP017483; AOX62949.1; -; Genomic_DNA.
DR   RefSeq; WP_070426636.1; NZ_CP017483.1.
DR   KEGG; slm:BIZ42_12475; -.
DR   KO; K01595; -.
DR   Proteomes; UP000177427; 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 {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000177427};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AOX62949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177427}.
FT   ACT_SITE    151    151       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    569    569       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   903 AA;  100025 MW;  C17FCB9E334414A4 CRC64;
     MNEYRSSIVF ATPDIPLRDD VRRLGALVGD LLAEQVSTQF FDDVEQVRTR AIARRESDAP
     LSDLNDALTG LPPARAEAMV RAFSTYFQVV NIAERVHRIR RRRDYQRAGT ATPQPDGLQD
     ALVNLKAQGV TLDELAEWLP RIDIEPVFTA HPTEAVRRAL LEKEQLMVAS LVDNLDGQRT
     PGEAAADAAR FRMALTASWQ TTDSSPVRPT VEDEREHVGF YLVQVLYRVI PVLYESLQQA
     LLDTYGQELP LPRLLRFGTW VGGDMDGNPN VDAGTIRNTL DAQRQAVLGR YQKDLLQLAS
     LLSQSTERVA VSDELQARVD HYKALLPKVT SRPRHADMPY RLLNDRMRAR VQATMDDAEG
     AYASPQELTD DIELILRSLH ENKGDHAGGF AVRRLLWRVR TFGFHLARLD VRQESSVHGR
     ALASVLDGQE AWDAADAVTR AARLAPFASG EQALPVSNEE GGERLDAVFA ALADAHHRHG
     ADALGSYIIS MAHDRSDVLA VLALARRGGL VDDAGAVPLD IAPLFETVDD LKRGTDTLRD
     LLADPVYRTH LASRGDVQMV MLGYSDSGKD GGIAASRWGL QRAQVELLEV AAENDIRLTF
     FHGRGGSISR GGGKTTHAVD ASPRGSIDGR LRVTEQGEVI HRKYGIRALA LRSLEQSTGA
     VLRSSLRPRA PEPREEQWRP VMDLIAQKSA DAYRVFVGQK DFMQYFRLAA PIDVIERMTL
     GSRPSRRLGE DAALTNLRAI PWVFAWSQAR AVIPGWYGVG SGLQAAIDAG HEDILKEMAR
     DWPFFSTFLD DIAMVLSKGD LTIAEQFSQL SGALHGRFFP QIQRELELTA QWILVLTGQD
     ALLQHDQRLA LSIRLRNPYI DPISVLQVDL LRRWRESGGE DDDVLRALVA CVNGVSQGVQ
     NTG
//
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