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Database: UniProt
Entry: A0A0Q9SSD7_9MICO
LinkDB: A0A0Q9SSD7_9MICO
Original site: A0A0Q9SSD7_9MICO 
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}.
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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
//
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