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Database: UniProt
Entry: A0A0B8NJN9_9NOCA
LinkDB: A0A0B8NJN9_9NOCA
Original site: A0A0B8NJN9_9NOCA 
ID   A0A0B8NJN9_9NOCA        Unreviewed;       322 AA.
AC   A0A0B8NJN9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:GAM48363.1};
DE   SubName: Full=Stearoyl-[acyl-carrier-protein] 9-desaturase {ECO:0000313|EMBL:APA97783.1};
DE            EC=1.14.19.2 {ECO:0000313|EMBL:APA97783.1};
GN   ORFNames=NS07_v2contig00071-0031 {ECO:0000313|EMBL:GAM48363.1},
GN   NS506_03734 {ECO:0000313|EMBL:APA97783.1};
OS   Nocardia seriolae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM48363.1, ECO:0000313|Proteomes:UP000019401};
RN   [1] {ECO:0000313|EMBL:GAM48363.1, ECO:0000313|Proteomes:UP000019401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N-2927 {ECO:0000313|EMBL:GAM48363.1,
RC   ECO:0000313|Proteomes:UP000019401};
RA   Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA   Oshima S.;
RT   "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT   Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT   quinqueradiata) in Kochi Prefecture, Japan.";
RL   Genome Announc. 3:e00082-15(2015).
RN   [2] {ECO:0000313|EMBL:APA97783.1, ECO:0000313|Proteomes:UP000180166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM150506 {ECO:0000313|EMBL:APA97783.1,
RC   ECO:0000313|Proteomes:UP000180166};
RA   Han H.-J.;
RT   "Genome sequence of Nocardia seriolae strain EM150506, isolated from
RT   Anguila japonica.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000346-1};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000346-1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000256|ARBA:ARBA00008749}.
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DR   EMBL; CP017839; APA97783.1; -; Genomic_DNA.
DR   EMBL; BAWD02000071; GAM48363.1; -; Genomic_DNA.
DR   RefSeq; WP_033088927.1; NZ_RCNK01000064.1.
DR   STRING; 37332.NS506_03734; -.
DR   KEGG; nsr:NS506_03734; -.
DR   PATRIC; fig|37332.12.peg.3840; -.
DR   OrthoDB; 9772881at2; -.
DR   Proteomes; UP000019401; Unassembled WGS sequence.
DR   Proteomes; UP000180166; Chromosome.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102786; F:stearoyl-[acp] desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01050; Acyl_ACP_Desat; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR005067; Fatty_acid_desaturase-2.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   PANTHER; PTHR31155; ACYL- ACYL-CARRIER-PROTEIN DESATURASE-RELATED; 1.
DR   PANTHER; PTHR31155:SF9; STEAROYL-[ACYL-CARRIER-PROTEIN] 9-DESATURASE 7, CHLOROPLASTIC; 1.
DR   Pfam; PF03405; FA_desaturase_2; 1.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|PIRSR:PIRSR000346-1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000346-1};
KW   Oxidoreductase {ECO:0000313|EMBL:APA97783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019401}.
FT   BINDING         76
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         199
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ   SEQUENCE   322 AA;  36703 MW;  DEE424E22B6A84AC CRC64;
     MARALTQREI LVELEPVAGQ ALDRHLSVFK EWHPHDYIPW EEGRNFAALG GTDWEPGQST
     LSEVAKAALV TNLLTEDNLP SYHREIAENF SRDGAWGSWV GRWTAEEARH SIVLRDYLVV
     TRGVDPVALE NDRMTHMTNG YTPPTGAAAL ADAGFLFSVT YVSFQELATR ISHRNTAKVC
     DDPIADRMLQ RLALDENLHM IFYRTLCGAA LDLVPDQAME AIDLIVENFR MPGTGMPNFR
     RHGVLMAKHG IYDLRQHLED VLQPVLRHWN IFDRNDFGPR GEQARERLAD FLNTMETVHI
     PRFEEHRDRA LARERDRATV AV
//
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