ID A0A0P0S8Z4_9PSEU Unreviewed; 381 AA.
AC A0A0P0S8Z4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Stearoyl-CoA 9-desaturase {ECO:0000313|EMBL:ALL80600.1};
GN ORFNames=AD017_04155 {ECO:0000313|EMBL:ALL80600.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL80600.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL80600.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL80600.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP012184; ALL80600.1; -; Genomic_DNA.
DR RefSeq; WP_060572994.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0S8Z4; -.
DR STRING; 1096856.AD017_04155; -.
DR KEGG; pecq:AD017_04155; -.
DR PATRIC; fig|1096856.3.peg.877; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000066228; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT DOMAIN 41..145
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 280..381
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 381 AA; 41284 MW; B389E97FA2B84C5C CRC64;
MSDTGTALPR GLRRARRAAA RFTTPLLPDD YLLLLNPLWS ARELRGRVVK IVRETSDAAT
LVIRPGLGWS FGHRAGQYVG IGVQVEGRFH WRSYSLTSEP RRDRRHISVT VKAMPEGFLS
KHLVDGVGPG TIVRLALPRG EFVLPDPPPS RLLFLTAGSG ITPIMAMLRT LDRRGTVPDT
VVVHSAPRSG DVIFAAELER LAQRHPSLRL HRHLTGERGR LTPDDLARYC PDWSERSTWA
CGPSAMLDEA EELWSSAGCD DRLHVERFSA SLRGGEAEGG TVTFARRGSA VAGTSTPDDG
DVAATVEIDG ATTLLEAGES ADLDLPYGCR MGICHTCVVG LRSGTVRDLR DGSEHRADPD
TPAEKVQTCV TAAAGDCVLE I
//
