ID E6J649_9ACTN Unreviewed; 754 AA.
AC E6J649;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:EFV92918.1};
GN ORFNames=ES5_03438 {ECO:0000313|EMBL:EFV92918.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV92918.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV92918.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV92918.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV92918.1}.
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DR EMBL; AEKG01000084; EFV92918.1; -; Genomic_DNA.
DR RefSeq; WP_007627458.1; NZ_AEKG01000084.1.
DR AlphaFoldDB; E6J649; -.
DR Proteomes; UP000004165; Unassembled WGS sequence.
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; cd00207; fer2; 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; 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; 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:SF6; NADH OXIDOREDUCTASE HCR; 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 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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 410..521
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 676..754
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 754 AA; 82853 MW; 6E743C0A0E4ED7F1 CRC64;
MTLAGSPDTA TDTGLAAELG ALYIRAKAAV GAEDLAHIRN VTAYGEAIDA RRRELLRDGG
PRAVRRATAL EMAYRLMQFS ELGHNIIHGS YDHLPDCGEY HSDRYHWDFN VDTDQWKTMH
HVGHHPNTNI VGKDHDLGYS LFRGSAGQDW YGHHLGQVVM ISTLAAMAPI AAPFFLANIA
RKVEGHGLFS SYMLRSPARI AGRDARRRFV DEPFRSGWKP LQTLAANYLG GVTGYMSVLF
LVFIEHHAGE LELFTDPGPD ETADQYYERQ IRATRNFLPS AQMDDALARL LEEEVPFENR
PDLRIFYGGL DTHVEHHLFP DLPPSMQRKI APEVREIAAR HGLPYHETPL LETVPLIAKT
LTGLSVPFGE REFSRPRDLL RDPASLVRRV AAGLRYRRLP ESPYLDKPQF HNVPARVVAA
TPVADGQALS VRLARPRGWE DVRWDAGAYV SVRQMVDDDE LVRQYSLVHD SVGQAGPSDL
QFCVKRVADG RVSNRLNDTL KPGAYVTLVG VPQSTGDFAL PAEPDTTHPA PTLHIAGGVG
ITPIIALLRR LARDAADSPA GAGPDATLLY FNRDERSIIF EPELRELARD AGITLHLFTD
APATRDDLRT GRLGPELLTE LVPDLAERET YVCAPAAVID LARGWLRGLG QPAERFHAES
FTAPELDRPA DDGSRYTVSF ARTGTSVEID GGTTLLEAAG RAGIPVPTGC ERGLCKACVT
TKLAGTTSAE QPGVQQERIT VCNSLASSDI ELDL
//
