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Database: UniProt
Entry: Q2W6R8_MAGSA
LinkDB: Q2W6R8_MAGSA
Original site: Q2W6R8_MAGSA 
ID   Q2W6R8_MAGSA            Unreviewed;       447 AA.
AC   Q2W6R8;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Predicted acyl-CoA transferase/carnitine dehydratase {ECO:0000313|EMBL:BAE50457.1};
GN   OrderedLocusNames=amb1653 {ECO:0000313|EMBL:BAE50457.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50457.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE50457.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family.
CC       {ECO:0000256|ARBA:ARBA00008383}.
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DR   EMBL; AP007255; BAE50457.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W6R8; -.
DR   STRING; 342108.amb1653; -.
DR   KEGG; mag:amb1653; -.
DR   HOGENOM; CLU_033975_0_0_5; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1540.10; formyl-coa transferase, domain 3; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   PANTHER; PTHR48207; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR   PANTHER; PTHR48207:SF3; SUCCINATE--HYDROXYMETHYLGLUTARATE COA-TRANSFERASE; 1.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; CoA-transferase family III (CaiB/BaiF); 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Transferase {ECO:0000313|EMBL:BAE50457.1}.
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  47559 MW;  411A4235BD9AF20D CRC64;
     MRIAAVRRHE GHQEDLADRP GLTLLSPGGS SPEPPVFSFS KDSIMTGPLS HLRVLDLSRV
     LAGPWAGQLL ADMGAEVIKV ERPGEGDDTR GWGPPFLKDG QGGDTGEAAY FLSANRGKRS
     VTIDFTQAQG QELVRRLAAR SDVVLENFKV GGLAKYGLDY ASLKAVKPDL VYCSITGFGQ
     DGPYAQRAGY DFLIQGMGGL MSLTGEPGGQ PMKVGVALTD IFTGMYAGFA ILAALAKRDR
     TGEGSQIDLA LLDVQVAVLA NQATNYLVGG ATPKRLGNAH PNIVPYQAFA TADGHIILAV
     GNDGQFRRFC HTAGRPELGA DPRFATNVER VRNRAELVPL LEALLTSRPS ARWIAELEEA
     GVPCGPINDL ANVFADPQVI HRGLRTRLDH PLAGGIDLVA NPIRFDGAQA LSDRAPPLLG
     ADTAEVLGGW LGMGADEMER LRENGVV
//
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