ID A0A0D1LBW9_9MYCO Unreviewed; 673 AA.
AC A0A0D1LBW9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Electron transfer flavoprotein {ECO:0000313|EMBL:KIU15712.1};
GN ORFNames=TL10_17635 {ECO:0000313|EMBL:KIU15712.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU15712.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU15712.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU15712.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-2015) 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:KIU15712.1}.
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DR EMBL; JXST01000024; KIU15712.1; -; Genomic_DNA.
DR RefSeq; WP_043986617.1; NZ_JXST01000024.1.
DR AlphaFoldDB; A0A0D1LBW9; -.
DR STRING; 280871.TL10_17635; -.
DR PATRIC; fig|280871.6.peg.3650; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000032221; 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; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 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; 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:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; 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; 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:UP000032221};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..430
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 584..673
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 673 AA; 74425 MW; F9770FF007BC8E6C CRC64;
MSPVEVVDRA DSQAGARQAL PDPGEQVPKL AWPTVALFLA GAVAFAASTV GYISGAVPTW
VPIVVNAVVT FTMFTVVHDA VHYAISSARW VNGLIGRLAV PFVQPLISFP SFGFIHIEHH
RHSNDDENDP DTFASHGPAW QLPFRWAVLD IWYGNYLIGK IRSRPKAEIA ETLACVTISV
TGLLVAIMSG HFWTLAVVFI IPQRIAVVVL AWWFDWMPHH GLEDTQRSDR YRATRTRVGM
EWLYTPLMLS QNYHLVHHLH PSVPFYRYTK TWRRNEEAYL DRGAAISTVF GQELNSDEFR
QWKQLNGNLG RALPVRMPDR SSAPHAVFHR IPVAAVDPIT ADSTLVTFAV PEALQDQFRF
EPGQHVSVRT DLGGEGVRRS YSICAPATRA QLRIAVKHIP GGTFSGFVAD QLKAGDVLEV
MTPAGSFSSA LHPLHRKHYV GLVAGSGITP VLSILATVME LETESRFTLI YGNRTTESTM
FRAELDRLES RYADRLEIRH VLSSEPMHIP ELSGRIDAER LTRWLTTDLH PETVDEWFLC
GPAAMSTGVR ETLIERGVDP EQIHLELFTG FDRADAPARD YQAATVTFRL SGKQQTVDVD
GGDTILEGAL QTGSSAPYSC MGGACGTCRA KLLTGTVEMD QNFALGRSDL DAGYILTCQS
HPTSPTVSVD YDA
//
