ID Q0S6I7_RHOJR Unreviewed; 391 AA.
AC Q0S6I7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Hydroxylase {ECO:0000313|EMBL:ABG96849.1};
GN OrderedLocusNames=RHA1_ro05068 {ECO:0000313|EMBL:ABG96849.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG96849.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2] {ECO:0007829|PDB:2OR0}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RA Tan K., Skarina T., Kagen O., Savchenko A., Edwards A., Joachimiak A.;
RT "The crystal structure of a putative hydroxylase from Rhodococcus sp.
RT RHA1.";
RL Submitted (FEB-2007) to the PDB data bank.
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DR EMBL; CP000431; ABG96849.1; -; Genomic_DNA.
DR RefSeq; WP_011597315.1; NC_008268.1.
DR PDB; 2OR0; X-ray; 2.10 A; A/B=1-391.
DR PDBsum; 2OR0; -.
DR AlphaFoldDB; Q0S6I7; -.
DR SMR; Q0S6I7; -.
DR KEGG; rha:RHA1_ro05068; -.
DR PATRIC; fig|101510.16.peg.5119; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_11; -.
DR OrthoDB; 3404950at2; -.
DR EvolutionaryTrace; Q0S6I7; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2OR0};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 235..365
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 391 AA; 42057 MW; 804EC24CD2A62E83 CRC64;
MGRVLDRIEV VAEEIRGQAV QSEADCRLTD AAAGLLRDSG AIRLLQPRLY GGYEVHPREF
AETVMGVAAL DGASGWVTGI VGVHPWELAF ADPQVQEEIW GEDNDTWMAS PYAPMGVATP
VDGGYVLKGR WSFSSGTDHC QWAFLGAMVG DGEGGIATPS SLHVILPRTD YQIVEDTWDV
IGLRGTGSKD LIVDGAFVPG YRTLNAAKVM DGRAQKEAGR PEPLFNMPYS CMFPLGITAA
VIGITEGALA CHIAVQKDRV AITGQKIKED PYVLSAIGES AAEINASRVS LIETADRFYD
KVDAGKEITF EERAIGRRTQ IAAAWRAVRA ADEIFARAGG GALHYKTPMQ RFWRDAHAGL
AHAVHVPGPT NHASALTQLG GEPQGMMRAM I
//
