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Database: UniProt
Entry: A0A172UR50_9MYCO
LinkDB: A0A172UR50_9MYCO
Original site: A0A172UR50_9MYCO 
ID   A0A172UR50_9MYCO        Unreviewed;       521 AA.
AC   A0A172UR50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Ferredoxin {ECO:0000313|EMBL:ANE81506.1};
GN   ORFNames=A7U43_21375 {ECO:0000313|EMBL:ANE81506.1};
OS   Mycobacterium adipatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE81506.1, ECO:0000313|Proteomes:UP000077143};
RN   [1] {ECO:0000313|EMBL:ANE81506.1, ECO:0000313|Proteomes:UP000077143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE81506.1,
RC   ECO:0000313|Proteomes:UP000077143};
RA   Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT   "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT   sp. YC-RL4.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000362-1};
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312}.
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DR   EMBL; CP015596; ANE81506.1; -; Genomic_DNA.
DR   RefSeq; WP_067999194.1; NZ_CP015596.1.
DR   AlphaFoldDB; A0A172UR50; -.
DR   STRING; 1682113.A7U43_21375; -.
DR   KEGG; madi:A7U43_21375; -.
DR   OrthoDB; 289202at2; -.
DR   Proteomes; UP000077143; Chromosome.
DR   GO; GO:0051536; F:iron-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:UniProtKB-KW.
DR   CDD; cd04410; DMSOR_beta-like; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000362-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077143}.
FT   DOMAIN          1..29
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          33..62
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         140
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         247..250
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         291..292
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         303
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         434..436
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         434
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   521 AA;  55864 MW;  B2351D04385382A9 CRC64;
     MAYVITQNCC KDASCVPVCP VDCIRPVHGG AADMLYIDPQ SCIDCGACFD ECPVGAIHYE
     EDLPAGQERF KDINAAYFTR HPLEADTTAA PPSRPGVAPG ELRVAVVGAG PAACYAAAEL
     IDIDGVEVNL FERLPTPFGL IRAGVAPDHQ HTKALVGIFE RIFANPRLGC HLGVEIGRDL
     SHDDLLAHHH AVIYAVGAGT SRQLGIPGEH LPGSHPAADF VGWYNGHPDH AGRTFDLGTE
     RAVIVGNGNV ALDVARILLT DQPRLSATDI AEHALESLRD SLIREVVILG RRGVADAAFS
     VGEFLALGHL DGVDVIIDGP LEDPAEGTDL WATLKLDIAR EYAERPVTPG NKRIVFRFMT
     SPVEIVGQDA VQALRTTGGD LDTGLVLRSI GYRGSAIDGL PFDEAAGLVP NVAGRVDGVP
     ATFVTGWIKR GPRGVIGTNR TCAEETVSQL WRDHLEGTLD RHVRGPDALR KLLQDRGVQA
     IDWQGWRAID TAERERGAAA SRPRVKFIGI PEMRTAALRS T
//
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