ID L7W548_NONDD Unreviewed; 334 AA.
AC L7W548;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Acyl-[acyl-carrier-protein] desaturase {ECO:0000313|EMBL:AGC76765.1};
GN OrderedLocusNames=DDD_1638 {ECO:0000313|EMBL:AGC76765.1};
OS Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS dokdonensis).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC76765.1, ECO:0000313|Proteomes:UP000011173};
RN [1] {ECO:0000313|EMBL:AGC76765.1, ECO:0000313|Proteomes:UP000011173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17205 / KCTC 12402 / DSW-6
RC {ECO:0000313|Proteomes:UP000011173};
RX PubMed=23292138; DOI=10.1093/gbe/evs134;
RA Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA Kim J.F.;
RT "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL Genome Biol. Evol. 5:187-187(2013).
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; CP001397; AGC76765.1; -; Genomic_DNA.
DR RefSeq; WP_015362262.1; NC_020156.1.
DR AlphaFoldDB; L7W548; -.
DR STRING; 592029.DDD_1638; -.
DR KEGG; ndo:DDD_1638; -.
DR PATRIC; fig|592029.3.peg.1624; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_034505_0_0_10; -.
DR OrthoDB; 9772881at2; -.
DR Proteomes; UP000011173; 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 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1"
SQ SEQUENCE 334 AA; 38740 MW; 07312F28384686E7 CRC64;
MNLPLKNKRI EVMQSLESKV ASFMDQYLIP VDKIWQPTDF LPNSQEDTFF EEVKELRELA
KELPYDFWVA LVGDTITEEA LPTYESWLMD VEGINQVEGK GNIWSKWVRQ WTGEENRHGD
VLNKYLYLSG RVNMREIEIT THHLLTDGFD IGTDRDPYKN FIYTSFQELA TYISHNRVAK
LARGYGNIAL SKMCRIISGD EMRHHKAYST FVTEIFKVDA SNMMIAFKEM MVHKIVMPAM
FLRESGQSIG AAFEDFSNSA QRIGVYTAQD YIDIMQKLID QWDIANMTHL TEEAEKARDY
LMKLPARMER VSQRIKIPEE SAKFSWVNPA LVGG
//
