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Database: UniProt
Entry: A0A1L7CWA9_9CORY
LinkDB: A0A1L7CWA9_9CORY
Original site: A0A1L7CWA9_9CORY 
ID   A0A1L7CWA9_9CORY        Unreviewed;       352 AA.
AC   A0A1L7CWA9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Stearoyl-CoA 9-desaturase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CSPHI_02715 {ECO:0000313|EMBL:APT90165.1};
OS   Corynebacterium sphenisci DSM 44792.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1437874 {ECO:0000313|EMBL:APT90165.1, ECO:0000313|Proteomes:UP000185469};
RN   [1] {ECO:0000313|EMBL:APT90165.1, ECO:0000313|Proteomes:UP000185469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44792 {ECO:0000313|EMBL:APT90165.1,
RC   ECO:0000313|Proteomes:UP000185469};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium sphenisci CECT 5990(T) (=DSM
RT   44792(T)), isolated from healthy wild penguins.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP009248; APT90165.1; -; Genomic_DNA.
DR   RefSeq; WP_075691388.1; NZ_CP009248.1.
DR   AlphaFoldDB; A0A1L7CWA9; -.
DR   STRING; 1437874.CSPHI_02715; -.
DR   KEGG; csph:CSPHI_02715; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000185469; 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; IPR006058; 2Fe2S_fd_BS.
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; PS00197; 2FE2S_FER_1; 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:UP000185469}.
FT   DOMAIN          33..137
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          272..352
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   352 AA;  37918 MW;  462C249CEDE16F28 CRC64;
     MSFTHRLKRA LEGFSTPLLP DDYTRLVNPL WSTREFRGRI VAVRRPTDTT AELVIRRGWG
     VPAEFRAGQH IGIGVRVDGR YVWRSYSLTC APQPADGLLT VTVKAIDDGR LSRHLVANAR
     PGIVVRLALP AGDFHLDEPV PEKLLFLTAG SGITPVMSML RDLRGRFGGG GPGAGPDVVH
     LHSARTAADV LFDAELAGMA RECGWYTRVL RLTGRQGRIT ARDLPGLVPD LAERQVYACG
     PAAMLDDVEA HVPGVRTERF ALDRGSTDAA GGMVVFPGRG EIEVDGATTI LEAGERAGIQ
     LPYGCRMGIC ATCVRQLADG TARDLRTGAT HEAGERIRVC VCVPAGDVEL EP
//
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