ID A0A176KZB2_9ACTN Unreviewed; 351 AA.
AC A0A176KZB2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Stearoyl-CoA 9-desaturase {ECO:0000313|EMBL:OAA97303.1};
GN ORFNames=A6P39_29120 {ECO:0000313|EMBL:OAA97303.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA97303.1};
RN [1] {ECO:0000313|EMBL:OAA97303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA97303.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-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:OAA97303.1}.
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DR EMBL; LWRP01000155; OAA97303.1; -; Genomic_DNA.
DR RefSeq; WP_067052276.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KZB2; -.
DR STRING; 710705.A6P39_29120; -.
DR OrthoDB; 9796486at2; -.
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 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 36..139
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 268..351
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 351 AA; 37920 MW; EC1C09CB686D7CD7 CRC64;
MTSAALRSRA WKMLEMVTTP LLPSDYLDLF SPLRAGADLR GRIEAVRPET GDAATIVIRP
GRGWRGHRAG QYVRIGVDVD GVRLWRAYSI TSPANRQDGR VTITVKAIPD GKVSNHLVCR
AKPGTLIQLD QATGDFVLPQ AKPAKVLYLT AGSGITPVMG MLRDTEFDDV VMVHCAPRPQ
DVIFRNELHD LVADKKLRLT EVHTDTDGML DIARLDELVP DWAERETWAC GPAGLLDAAE
EHWSEHGVQE RLHTERFRPG IVVAGDGGEV TFSATGKTVD ADGATPLLDI GEEAGVLMPS
GCRMGICFGC VTPLKAGAVR DLRTGEITEA EPGVLIQTCV SAAAGPCDIE R
//
