ID A6GLB3_9BURK Unreviewed; 756 AA.
AC A6GLB3;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:EDM84794.1};
GN ORFNames=LMED105_04577 {ECO:0000313|EMBL:EDM84794.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84794.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM84794.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84794.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDM84794.1}.
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DR EMBL; ABCT01000001; EDM84794.1; -; Genomic_DNA.
DR RefSeq; WP_008247232.1; NZ_ABCT01000001.1.
DR AlphaFoldDB; A6GLB3; -.
DR STRING; 391597.LMED105_04577; -.
DR OrthoDB; 4759734at2; -.
DR Proteomes; UP000010322; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03512; Alkane-hydroxylase; 1.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06213; oxygenase_e_transfer_subunit; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR033885; AlkB/XylM.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 372..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..99
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 103..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 756 AA; 84486 MW; 9F78A4B3E777E5BF CRC64;
MLQFLNKGST HKANINGKLI HVEADETLLL AALRQNVEIP NICRVGGCGS CKCKLKDGRV
QELTESAYLL SEEEIAEGYI LACQSRLKSD IEVEMDESAA ITSSPVAGRI VKREFLTHDI
ARIDVQLDQP INYKAGQFAE LTLDSVKNAP RSYSFSNAPD NQGLASFTIR RVPSGRFSTY
VFDKLVEGEI LTVRGPGGDF WLREGGEKVV FIAGGSGLAP ILGMLEEMER KGDRRPVTLL
FGARTEQDLY ELHRLDAYTK NWPGFRFVPI LSEDNSNHNW NGLRGLVTDH IRREAAGATQ
AYLCGPPQMI DAAIKELKEN KLAAQGIYAD RFVVREVMNT GFYGAVGLPL IERTPATIGD
YLKFMMFHLM GVIAVVAYLA GGAWITAGFA SLLGFYVLGD MLTGDDTVTP EYRKPWILTV
QLWLALPLLL LIGFCFMWTM STGDPLGLGE FVMGLTSYDV FAAREATSSV HRYFSGIIYY
GYLIGIMGTV VAHELTHRTW DPVSLWVGRW LLAFSYDAGF AIEHVYGHHR YVSTEHDPAT
APRGRNVYLH IVLSTIKGNI SAAKIEAERL NKKGLPVMSY HNAYIRGLLM SVVLNVAAFS
VAGWTGALCF SLAALFGKSL LEIVNYMEHY GMVRLPEQPV QPRHSWNTNR RMTSWGMFNL
SRHSHHHAQG EVPYQNLMPL PDAPVMIGGY LTTIFLTLCP PLWHKLMTSK LVEWDRHFAS
PEEQILALRA NQRSGIKELV DYDPRQWSLD SIKYST
//
