ID F0SCJ3_PSESL Unreviewed; 327 AA. AC F0SCJ3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 58. DE SubName: Full=Acyl-(Acyl-carrier-protein) desaturase {ECO:0000313|EMBL:ADY52827.1}; DE EC=1.14.19.2 {ECO:0000313|EMBL:ADY52827.1}; GN OrderedLocusNames=Pedsa_2278 {ECO:0000313|EMBL:ADY52827.1}; OS Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG OS 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans). OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pseudopedobacter. OX NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY52827.1, ECO:0000313|Proteomes:UP000000310}; RN [1] {ECO:0000313|EMBL:ADY52827.1, ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; RX PubMed=22180808; DOI=10.4056/sigs.2154937; RA Liolios K., Sikorski J., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Huntemann M., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., RA Kotsyurbenko O., Rohde M., Tindall B.J., Abt B., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of the gliding, heparinolytic Pedobacter saltans RT type strain (113)."; RL Stand. Genomic Sci. 5:30-40(2011). RN [2] {ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Pedobacter saltans DSM 12145."; RL Submitted (FEB-2011) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002545; ADY52827.1; -; Genomic_DNA. DR AlphaFoldDB; F0SCJ3; -. DR STRING; 762903.Pedsa_2278; -. DR KEGG; psn:Pedsa_2278; -. DR eggNOG; COG0208; Bacteria. DR HOGENOM; CLU_034505_0_0_10; -. DR OrthoDB; 9772881at2; -. DR Proteomes; UP000000310; 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:ADY52827.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000310}. 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 113 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1" FT BINDING 113 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1" FT BINDING 116 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 199 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="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1" FT BINDING 202 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000346-1" SQ SEQUENCE 327 AA; 37439 MW; BFC93C0953533252 CRC64; MHELSVGSRR EVMTYLEPFM LGEMADYLKP VEEMWQPADF LPDASKDTFF DEVKELQEST KELSYDLLAV LIGDTITEEA LPTYESWLTM VDDVSKSEQG GWMKWVRAWT AEENRHGDLL NKYLYLSGRI NMRAMEISTQ YLIQDGFDIG TGADPYRNFI YTSFQEMATN VSHRRVAALA KKAGDKLLSK MCGVIAADEA RHAKAYKSFI SKAMEVDASQ VMIAFEDMMR KKIVMPAHFL REIGLKMGET FGHFTDAAQR LGVYTAVDYV DILKELNNDW NIANVTGLDE AGEKARDYLM ALPNRLLRVA ERIKVPELEY KFSWIHS //