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Database: UniProt
Entry: U5WN98_MYCKA
LinkDB: U5WN98_MYCKA
Original site: U5WN98_MYCKA 
ID   U5WN98_MYCKA            Unreviewed;       338 AA.
AC   U5WN98;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Acyl-ACP desaturase {ECO:0000313|EMBL:AGZ50683.1};
GN   ORFNames=MKAN_10655 {ECO:0000313|EMBL:AGZ50683.1};
OS   Mycobacterium kansasii ATCC 12478.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ50683.1, ECO:0000313|Proteomes:UP000017786};
RN   [1] {ECO:0000313|EMBL:AGZ50683.1, ECO:0000313|Proteomes:UP000017786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ50683.1,
RC   ECO:0000313|Proteomes:UP000017786};
RG   McGill University Mycobacterium genome consortium;
RA   Veyrier F.J., Behr M.A.;
RT   "Genome sequence of Mycobacterium kansasii.";
RL   Submitted (OCT-2013) 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; CP006835; AGZ50683.1; -; Genomic_DNA.
DR   RefSeq; WP_023367951.1; NC_022663.1.
DR   AlphaFoldDB; U5WN98; -.
DR   GeneID; 29702376; -.
DR   KEGG; mkn:MKAN_10655; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_034505_3_0_11; -.
DR   OrthoDB; 9772881at2; -.
DR   Proteomes; UP000017786; Chromosome.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT   COILED          275..313
FT                   /evidence="ECO:0000256|SAM:Coils"
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="2"
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         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT   BINDING         200
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ   SEQUENCE   338 AA;  39019 MW;  1B0A421F98FCA0E9 CRC64;
     MSAQLTDLQL LHELEPVVEK YLNRHISMHK NWNPHDYIPW SDGKNYYALG GQDWDPEESK
     LSDVAQVAMV QNLVTEDNLP SYHREIAMNM GMDGAWGQWV NRWTAEENRH GIALRDYLVV
     TRSVDPVELE KLRLEVVNRG FSPGQNHQGE YFAESVTDSV IYVSFQELAT RVSHRNTGKA
     CNDPVADQLM ARISADENLH MIFYRDVSEA AFDLAPNQAM KSLHLILRHF KMPGFLVPEF
     RRKAVIIAVG GVYDIRIHLD EVVKPVLKKW RIFERDDFTG EAAQMRDDLA KLMEELEAEC
     DKFEASKQRY LARQARMDER ITARKVLTTK GTLRMTGR
//
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