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Database: UniProt
Entry: A0A1A2UYF9_MYCSC
LinkDB: A0A1A2UYF9_MYCSC
Original site: A0A1A2UYF9_MYCSC 
ID   A0A1A2UYF9_MYCSC        Unreviewed;       365 AA.
AC   A0A1A2UYF9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Stearoyl-CoA 9-desaturase {ECO:0000313|EMBL:OBH93601.1};
GN   ORFNames=A5679_22930 {ECO:0000313|EMBL:OBH93601.1};
OS   Mycobacterium scrofulaceum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1783 {ECO:0000313|EMBL:OBH93601.1, ECO:0000313|Proteomes:UP000092207};
RN   [1] {ECO:0000313|EMBL:OBH93601.1, ECO:0000313|Proteomes:UP000092207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2838 {ECO:0000313|EMBL:OBH93601.1,
RC   ECO:0000313|Proteomes:UP000092207};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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:OBH93601.1}.
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DR   EMBL; LZJY01000322; OBH93601.1; -; Genomic_DNA.
DR   RefSeq; WP_067276609.1; NZ_LZJY01000322.1.
DR   AlphaFoldDB; A0A1A2UYF9; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000092207; 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; 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; PR00410; PHEHYDRXLASE.
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          11..146
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          283..365
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   365 AA;  40594 MW;  70FAFEB6EFFCC15B CRC64;
     MAERGAEPQV PRGRRLFLRA VRRLFSPLQP DDYLEMINPL WTTKELRGKV EAIEQQGSEA
     ASVLIRPGYE WPGHKPGQYV RLGVVIDGVY HWRAYSLTSD PTPEDGLISV TPKRVDGGAV
     SPYLVHKIQP GDLVRLGEIE GVFTLPEPLP DKMLFISAGS GITPIISMLR DLDHRDEMRD
     AVVIHSARTR EQAMFLPALE ELEKRHQGMR LDLRFTSEQG RLTPGDLDDV CPDWREREAF
     CSGPGEMLDA LIEHWENNGD RDRLHFERFQ PKIGGDANAG EGGTVCFLDS DKEVECDGGT
     SILEAGEKAG LNLAYGCRIG ICHTCVGTLK SGKLRDLRSG DVIEPTEQDV RICINTAEGD
     VELEL
//
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