ID A0A024JVJ2_9MYCO Unreviewed; 383 AA.
AC A0A024JVJ2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=2Fe-2S iron-sulfur cluster binding domain-containing protein {ECO:0000313|EMBL:CDO87382.1};
GN ORFNames=BN973_01735 {ECO:0000313|EMBL:CDO87382.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO87382.1};
RN [1] {ECO:0000313|EMBL:CDO87382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO87382.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO87382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO87382.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; HG964446; CDO87382.1; -; Genomic_DNA.
DR RefSeq; WP_036467287.1; NZ_LQPY01000024.1.
DR AlphaFoldDB; A0A024JVJ2; -.
DR STRING; 47839.BN973_01735; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_2_11; -.
DR OrthoDB; 9796486at2; -.
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 CDD; cd00207; fer2; 1.
DR CDD; cd06216; FNR_iron_sulfur_binding_2; 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; 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; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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; 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 58..167
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 302..383
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 383 AA; 41315 MW; 870A3E19FD48A7C7 CRC64;
MGRKYQSLTA NVVDTKRPTV AGAERHPGWH ALRKIAARIT TPLLPDDYLQ LANPLWSARE
LRGRIVQVRR ETEDSATLVI KPGWGFSFDF EPGQYIGIGL RINGRWRWRS YSLTSSPVAR
SGSGPERTVT ITVKAMPEGF LSSHLVAGVE PGTIVRLAAP QGNFVLPDPA PPSILFLTAG
SGITPVMSML RTLVRRNQIG DIQHVHSAPT GSDVMFGSEL TALASVHPGY RLQVRETRTR
GRLDLARLDD EVPDWRQRQT WACGPEGMLA QAEKVWAAAG IGDRLHLERF AVAKAAPAGA
GGTVTFGRSG RTVTADAATS LMDAGEGAGI QMPFGCRMGI CQSCVVPLLD GHVRDLRTGQ
EHEPGSRVQT CISAASGDCV LDI
//
