ID A0A059MUN7_9NOCA Unreviewed; 318 AA.
AC A0A059MUN7; A0A0F6VGJ6; N1M403;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acyl-ACP desaturase {ECO:0000313|EMBL:UYF93401.1};
GN ORFNames=OCS65_23665 {ECO:0000313|EMBL:UYF93401.1};
OS Rhodococcus aetherivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=191292 {ECO:0000313|EMBL:UYF93401.1, ECO:0000313|Proteomes:UP001163947};
RN [1] {ECO:0000313|EMBL:UYF93401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N1 {ECO:0000313|EMBL:UYF93401.1};
RA Jiang W.;
RT "The genome sequence of Rhodococcus aetherivorans N1.";
RL Submitted (SEP-2022) 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; CP106982; UYF93401.1; -; Genomic_DNA.
DR RefSeq; WP_006936396.1; NZ_JAWLKG010000006.1.
DR GeneID; 83623481; -.
DR KEGG; rav:AAT18_05330; -.
DR Proteomes; UP001163947; 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 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 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 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ SEQUENCE 318 AA; 36358 MW; EAD85EFEBF4E4944 CRC64;
MTRVLTQLEL LRELEPVAEA NVNRHLSMAK DWHPHDYVPW DEGRNFAAMG GVDWEPEQSK
LDEVAKAAMI TNLLTEDNLP SYHREIAESF SRDGAWGTWV GRWTAEENRH GIVMRDYLVV
TRGVDPVALE NARMEHMTNG FASPNEVGML HSVSYVTFQE LATRVSHRNT GRACHDSIAD
KMLQRIAADE NLHMIFYRNI CEAALDVAPD QTLAAITDVL KNFQMPGAGM PNFRRNGVLM
AKHGIYDLRQ HLDEVVMPVL RKWRIFERED FGAEGARILD ELGTFLEDLE KQAVKFEEMR
DRSLAREAAR RERNEAAS
//
