ID A1T9Y2_MYCVP Unreviewed; 365 AA.
AC A1T9Y2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:ABM13982.1};
GN OrderedLocusNames=Mvan_3180 {ECO:0000313|EMBL:ABM13982.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM13982.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM13982.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM13982.1; -; Genomic_DNA.
DR RefSeq; WP_011780387.1; NZ_JACKSD010000379.1.
DR AlphaFoldDB; A1T9Y2; -.
DR STRING; 350058.Mvan_3180; -.
DR KEGG; mva:Mvan_3180; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_11; -.
DR Proteomes; UP000009159; Chromosome.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 52..152
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 280..365
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 365 AA; 38585 MW; 99C399EB3DB0DF32 CRC64;
MTRLFSQFRQ TPPSPSGRLR HDVMLGIAET AIAGMFAASA AVRRVRMPAA GPDTIPLTVT
GRRVVAHDQD VVELTLAGDR LPRWFPGAHL DVHLPSGRVR QYSLCGDPDS AEYRIAVRRI
PDGGGGSVEV HDALEIGSTV HTHGPRNAFP LTVPGYGSPA RRFRFIAGGI GITPILPMLG
LARRLGVDWS MVYTGRSVDS LPFVDEVTAF GAAVDIRTDD RHGLPAAAEL LGDCADGTAV
YACGPAPMLT AVRAALVGRD DVELHFERFA APPVTDGRPF QATVASTGQQ VDVGADETLL
AALRRAGVDA SYSCQQGFCG TCRTRVLAGS VEHRDTLLTG PERAAGLMLT CVSRAGDGSG
LTLDL
//
