ID A0A0Q9SSD7_9MICO Unreviewed; 369 AA.
AC A0A0Q9SSD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Stearoyl-CoA 9-desaturase {ECO:0000313|EMBL:KRF27318.1};
GN ORFNames=ASG91_12705 {ECO:0000313|EMBL:KRF27318.1};
OS Phycicoccus sp. Soil802.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF27318.1, ECO:0000313|Proteomes:UP000050906};
RN [1] {ECO:0000313|EMBL:KRF27318.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF27318.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF27318.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF27318.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRF27318.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMSS01000005; KRF27318.1; -; Genomic_DNA.
DR RefSeq; WP_056922990.1; NZ_LMSS01000005.1.
DR AlphaFoldDB; A0A0Q9SSD7; -.
DR Proteomes; UP000050906; 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 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:ARBA00022723}.
FT DOMAIN 50..153
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 284..369
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 369 AA; 39372 MW; C7EBECEF38F54B5D CRC64;
MSAVLPLRTT SGSTSPLPSL RTVLRRVAEA VATPVLPDDY LDLIAPMRAG ADLRGRVVSV
TPETRDAATV HIRPGRSWAG FVPGQYIRIG VDVDGVRNWR AYSLTSPLNS PDGLISITVK
AIPDGKVSNH VVRALQPGTL IHLDQATGEF VLPTPRPARA LFVTAGSGVT PVMGMLRNHL
DELHDVVVIH SAPTEADVIF AAELREWAEA GRIRLVERHT DTEGMVGADS LDELVPDWRF
RETWACGPTG MLDAFEAAWA DAEITDRLHT ERFRPVIIAE GEGGTVTFGG QRITVDADGS
TPILDAGEAA GVLMPSGCRM GICFGCVVPL KEGAVRDLRN GDLTIAAEGD GIRIQTCVSA
AAGHCEIDL
//