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Database: UniProt/TrEMBL
Entry: A0A0D5V9F1_9BURK
LinkDB: A0A0D5V9F1_9BURK
Original site: A0A0D5V9F1_9BURK 
ID   A0A0D5V9F1_9BURK        Unreviewed;      1043 AA.
AC   A0A0D5V9F1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-NOV-2017, entry version 22.
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=OI25_663 {ECO:0000313|EMBL:AJZ58706.1};
OS   Paraburkholderia fungorum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=134537 {ECO:0000313|EMBL:AJZ58706.1, ECO:0000313|Proteomes:UP000032614};
RN   [1] {ECO:0000313|EMBL:AJZ58706.1, ECO:0000313|Proteomes:UP000032614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-463 {ECO:0000313|EMBL:AJZ58706.1,
RC   ECO:0000313|Proteomes:UP000032614};
RX   PubMed=25931592;
RA   Johnson S.L., Bishop-Lilly K.A., Ladner J.T., Daligault H.,
RA   Jaissle J., Frey K.G., Koroleva G.I., Bruce D.C., Coyne S.R.,
RA   Broomall S.M., Li P., Teshima H., Gibbons H.S., Palacios G.F.,
RA   Rosenzweig C.N., McMurry K., Redden C.L., Xu Y., Currie B., Mayo M.,
RA   Minogue T.D., Chain P.S.;
RT   "Complete genome sequences for 59 burkholderia isolates, both
RT   pathogenic and near neighbor.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
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; CP010026; AJZ58706.1; -; Genomic_DNA.
DR   RefSeq; WP_046566404.1; NZ_CP010026.1.
DR   EnsemblBacteria; AJZ58706; AJZ58706; OI25_663.
DR   KEGG; bfn:OI25_663; -.
DR   PATRIC; fig|134537.4.peg.722; -.
DR   KO; K01595; -.
DR   Proteomes; UP000032614; Chromosome 1.
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:UP000032614};
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:AJZ58706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032614}.
FT   ACT_SITE    253    253       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    695    695       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1043 AA;  114363 MW;  1BFDDA87025D37A7 CRC64;
     MTSSGSARPA RRNTASPNAQ AADAASASAS AATAAQSTPA KRAGKAGKTS QPANVAKTAR
     SAKTAAKANK AVKDVKIEKV AQAAKAPKLQ AVSQDAAVPA PAPKSSARTR EDKDHPLFQD
     IRYLGRLLGD VLREQEGDAV FDVVETIRQT AVRFRREDDN AAAQTLDKKL RSLSPEQTVS
     VVRAFSYFSH LANIAEDRHR NRRHRIHALA GSTSQPGTMA HTLERLVAAG AAATPVLQQF
     FNEALIVPVL TAHPTEVQRK SILDAQHDVA RLLAERDQPL TDRERAHNEA MLRARVTSLW
     QTRMLRDSRL SVADEIENAL SYYRATFLEE IPALYADIEE ALTEHGIDAR LPPFFQMGSW
     IGGDRDGNPN VTAETLENAI TRQAAVIFEH YMEQVHKLGA ELSVSNLLAG ASDELKALAA
     ASPDQSPHRT DEPYRRALIG MYTRLAASAR VRLGEGSVPV RSAGRGAAPI RAIPYDDSAD
     FVRDLHVLID SLAAHHGAPL AAPRLSPLAR AAEVFGFHLA SIDLRQSSDI HEAVVAELLK
     RAGVENDYAS LAEEDKLKVL LAELSQPRPL RLPYTEYSDL VKSELGVLEE ARVTREKFGL
     RAVRNYIISH TETVSDLVEV MLLQKETGLL QGRLGDANDP ARAGLMVIPL FETIPDLRNA
     PHIMRDLIAL PGMDALIEHQ GNEQEVMLGY SDSNKDGGFL TSNWELYRAE LALVSLFNQR
     GVTLRLFHGR GGTVGRGGGP TYQAILSQPP GTVDGQIRLT EQGEVIASKF GNPEIGRRNL
     ETVVAATLEA SLLPHGIAPA QLPAFEETMQ QLSDAAMASY RALVYETPGF KEYFFESTPI
     SEIAELNIGS RPASRKLQDP KQRKIEDLRA IPWGFSWGQC RLLLTGWYGF GSAVAAHLDG
     APSDAERARR LALLKKMHKT WPFFSNLLSN MDMVLAKTDL AVASRYAQLV TDKKLRKHVF
     ERIVAEWERT SKVLSEITGK SERLAENPLL ARSIKNRFPY LDPLNHLQVE LLKRHRAGDT
     NARVRRGIHL TINGIAAGLR NTG
//
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