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Database: UniProt
Entry: X8CNS7_MYCIT
LinkDB: X8CNS7_MYCIT
Original site: X8CNS7_MYCIT 
ID   X8CNS7_MYCIT            Unreviewed;       313 AA.
AC   X8CNS7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=2Fe-2S iron-sulfur cluster binding domain protein {ECO:0000313|EMBL:EUA56905.1};
GN   ORFNames=I550_0021 {ECO:0000313|EMBL:EUA56905.1};
OS   Mycobacterium intracellulare 1956.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA56905.1, ECO:0000313|Proteomes:UP000020825};
RN   [1] {ECO:0000313|EMBL:EUA56905.1, ECO:0000313|Proteomes:UP000020825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1956 {ECO:0000313|EMBL:EUA56905.1,
RC   ECO:0000313|Proteomes:UP000020825};
RA   Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-2013) 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:EUA56905.1}.
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DR   EMBL; JAOG01000001; EUA56905.1; -; Genomic_DNA.
DR   AlphaFoldDB; X8CNS7; -.
DR   PATRIC; fig|1299331.3.peg.21; -.
DR   Proteomes; UP000020825; 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   CDD; cd00207; fer2; 1.
DR   CDD; cd06185; PDR_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; 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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT   DOMAIN          1..98
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          228..313
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   313 AA;  33895 MW;  F1A369C92AFC91DD CRC64;
     MRVERARREA REVISLRLVH PRGLLLPAWT PGAHIDVILP SGKVRQYSLC GDPTDRGAYT
     VAVLREPAGR GGSIEIHDPA LVGRDVGVSQ PRNHFPLVEA ERYLFIAGGI GITPILPMAR
     VVEARGIPWR LVYGGRARDS MAFVTDVKAL GGNRVELCPQ NETGVLDVES IVGNASTDTA
     MYCCGPEGLI KAVESACQRH LPPGSLHVER FAPSDPSSTR PQEPGKGFDV ELRRTGVVLH
     VPPDRSLLDV VREAVPTVLS SCEEGFCGAC VTTVLDGLPE HHDTVLTDAE RKNNDTMIIC
     VGRAKSERLV LDL
//
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