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
//