ID A0A1R0U7N4_9MYCO Unreviewed; 387 AA.
AC A0A1R0U7N4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Stearoyl-CoA 9-desaturase {ECO:0000313|EMBL:OMC13766.1};
GN ORFNames=A5736_22265 {ECO:0000313|EMBL:OMC13766.1};
OS Mycobacterium sp. SP-6446.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834162 {ECO:0000313|EMBL:OMC13766.1, ECO:0000313|Proteomes:UP000187139};
RN [1] {ECO:0000313|Proteomes:UP000187139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-6446 {ECO:0000313|Proteomes:UP000187139};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMC13766.1}.
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DR EMBL; MBEM01000158; OMC13766.1; -; Genomic_DNA.
DR RefSeq; WP_076246955.1; NZ_MBEM01000158.1.
DR AlphaFoldDB; A0A1R0U7N4; -.
DR Proteomes; UP000187139; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06216; FNR_iron_sulfur_binding_2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 58..171
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 306..387
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 387 AA; 41519 MW; D749C4A954412E9D CRC64;
MSKQHASIAA NVVDTKRPSV VGAERHPGWH ALRKLAARIT TPLLPDDYLH LANPLWSARE
LRGRILEVRR ETEDSATLVI KPGWGFSFDY QPGQYMGIGL LVDGRWRWRS YSLTSSPAET
SRSALGSGAA RTVTITVKAM PEGFLSSHLV AGVEPGTIVR LAAPQGNFVL PDPAPASILF
LTAGSGITPV MSMLRTLARR DQITDIAHLH SVPTESDMMF GAELSELAAD QPGYRLRVRE
TRTQGRLDLG SLDGEVPDWR QRHTWACGPE GLLNQAERVW SAAGIGDRLH LERFAVSKAA
PAGAGGTVTF ARSGRAVAAD AATSLMDAGE GAGVQMPFGC RMGICQSCVV SLVEGHVRDL
RTGKEHDPGT RVQTCISAAS GDCVIDI
//
