(data stored in ACNUC29543 zone)

SWISSPROT: B2JM63_PARP8

ID   B2JM63_PARP8            Unreviewed;       415 AA.
AC   B2JM63;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Formyl-CoA:oxalate CoA-transferase {ECO:0000256|HAMAP-Rule:MF_00742};
DE            Short=FCOCT {ECO:0000256|HAMAP-Rule:MF_00742};
DE            EC=2.8.3.16 {ECO:0000256|HAMAP-Rule:MF_00742};
DE   AltName: Full=Formyl-coenzyme A transferase {ECO:0000256|HAMAP-Rule:MF_00742};
DE            Short=Formyl-CoA transferase {ECO:0000256|HAMAP-Rule:MF_00742};
GN   Name=frc {ECO:0000256|HAMAP-Rule:MF_00742};
GN   OrderedLocusNames=Bphy_3614 {ECO:0000313|EMBL:ACC72753.1}, Bphy_4694
GN   {ECO:0000313|EMBL:ACC73803.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72753.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|EMBL:ACC72753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=STM815 {ECO:0000313|EMBL:ACC72753.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D.,
RA   Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Bacher J., Blanchard J., Cohan F.,
RA   James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P.,
RA   Riley M., Souza V., Wertz J., Young P.;
RT   "Complete sequence of chromosome2 of Burkholderia phymatum STM815.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- FUNCTION: Involved in the catabolism of oxalate and in the
CC       adapatation to low pH via the induction of the oxalate-dependent
CC       acid tolerance response (ATR). Catalyzes the transfer of the CoA
CC       moiety from formyl-CoA to oxalate. {ECO:0000256|HAMAP-
CC       Rule:MF_00742}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formyl-CoA + oxalate = formate + oxalyl-CoA;
CC         Xref=Rhea:RHEA:16545, ChEBI:CHEBI:15740, ChEBI:CHEBI:30623,
CC         ChEBI:CHEBI:57376, ChEBI:CHEBI:57388; EC=2.8.3.16;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00742};
CC   -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation;
CC       CO(2) and formate from oxalate: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00742}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00742}.
CC   -!- SIMILARITY: Belongs to the CaiB/BaiF CoA-transferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00742}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00742}.
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DR   EMBL; CP001044; ACC72753.1; -; Genomic_DNA.
DR   EMBL; CP001044; ACC73803.1; -; Genomic_DNA.
DR   RefSeq; WP_012402926.1; NC_010623.1.
DR   STRING; 391038.Bphy_4694; -.
DR   EnsemblBacteria; ACC72753; ACC72753; Bphy_3614.
DR   EnsemblBacteria; ACC73803; ACC73803; Bphy_4694.
DR   GeneID; 27744335; -.
DR   KEGG; bph:Bphy_3614; -.
DR   KEGG; bph:Bphy_4694; -.
DR   eggNOG; ENOG4105C04; Bacteria.
DR   eggNOG; COG1804; LUCA.
DR   HOGENOM; HOG000219745; -.
DR   KO; K07749; -.
DR   OMA; DTKNPKG; -.
DR   OrthoDB; 969868at2; -.
DR   BioCyc; BPHY391038:G1GBS-3710-MONOMER; -.
DR   BioCyc; BPHY391038:G1GBS-4788-MONOMER; -.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0033608; F:formyl-CoA transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033611; P:oxalate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   HAMAP; MF_00742; Formyl_CoA_transfer; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_sf.
DR   InterPro; IPR017659; Formyl_CoA_transfer.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
DR   TIGRFAMs; TIGR03253; oxalate_frc; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JM63.
DR   SWISS-2DPAGE; B2JM63.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00742,
KW   ECO:0000313|EMBL:ACC72753.1}.
FT   REGION       17     18       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   REGION       96     98       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   REGION      136    139       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   REGION      247    249       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   ACT_SITE    168    168       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00742}.
FT   BINDING      38     38       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_00742}.
FT   BINDING     104    104       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_00742}.
SQ   SEQUENCE   415 AA;  45538 MW;  8871C10A6D413545 CRC64;
     MGKALDGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERAG AGDITREQLR DIPDADSLYF
     TMLNHNKRSV TIDTKNPEGK LVLEALIQKC DVMVENFAPG ALDRMGFTWE RIQELNPKMI
     VASVKGFGPG PYEDCKVYEN VAQCVGGAAS TTGFDDGPPV VTGAQIGDSG TGLHLALGIV
     TALYQRTMTG RGQKVLAAMQ DGVLNLCRVK LRDQQRLQRT GVMKEYPQYP NGTFGEAVPR
     AGNASGGGQP GWILKCKGWE HDPNAYIYFI TQAPVWVKIC NVIGKEEWAT DADYATPNAR
     LPRLKEIFAE IERWTMTKTK FEAMEILNRH DIPCGPILSM KEIMDDESLR KTGTIVEVDH
     PVRGKYLTVG NPIKLSDSPT EVTRSPLLGE HTDEVMAELG YSPAQIEALR TAGAI
//

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