(data stored in ACNUC7421 zone)

SWISSPROT: Q13RQ4_PARXL

ID   Q13RQ4_PARXL            Unreviewed;       416 AA.
AC   Q13RQ4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 74.
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   ORFNames=Bxe_B2760 {ECO:0000313|EMBL:ABE33235.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33235.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33235.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33235.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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: Formyl-CoA + oxalate = formate + oxalyl-CoA.
CC       {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; CP000271; ABE33235.1; -; Genomic_DNA.
DR   RefSeq; WP_007178896.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13RQ4; -.
DR   STRING; 266265.Bxe_B2760; -.
DR   EnsemblBacteria; ABE33235; ABE33235; Bxe_B2760.
DR   GeneID; 4006524; -.
DR   KEGG; bxb:DR64_5093; -.
DR   KEGG; bxe:Bxe_B2760; -.
DR   eggNOG; ENOG4105C04; Bacteria.
DR   eggNOG; COG1804; LUCA.
DR   HOGENOM; HOG000219745; -.
DR   KO; K07749; -.
DR   OMA; KFDIPCA; -.
DR   OrthoDB; POG091H08U4; -.
DR   BRENDA; 2.8.3.16; 7691.
DR   UniPathway; UPA00540; UER00598.
DR   Proteomes; UP000001817; 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.
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; Q13RQ4.
DR   SWISS-2DPAGE; Q13RQ4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00742,
KW   ECO:0000313|EMBL:ABE33235.1}.
FT   REGION       15     18       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   REGION       72     75       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      137    140       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   REGION      248    250       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00742}.
FT   ACT_SITE    169    169       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   416 AA;  45812 MW;  B57AF4BD06572333 CRC64;
     MTKPLEGIRI IDFTHVQAGP ACTQLLAWFG ADVIKVERPG SGDVTRNQLR DIPDADALYF
     TMLNSNKKSL TLDTKKPEGK EVLEKLIRES DVLVENFGPG ALDRMGFSWE RLNELNPKMI
     VASVKGFSDG HHYDDLKVYE NVAQCAGGAA STTGFWDGPP TISAAALGDS NTGMHLAIGI
     LTALLGRDKT GKGQKVAVSM QDSVLNLCRV KLRDQQRLER VGYLEEYPQY PHGEFSDVVP
     RGGNAGGGGQ PGWVLKCKGW ETDPNAYIYF TIQGHAWEPI CKALGKPEWI DDPAYKTAEA
     RQPHIFDIFQ TIETWLADKT KFEAVDILRK FDIPCAPVLT MKELANDPSL RASGTIVEVP
     HKKRGTYLTV GSPIKFSDLK PEVTASPLLG EHTDEVLASL GYSQQQIFNL REVKAV
//

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