ID A0A098Y8A8_9ACTN Unreviewed; 325 AA.
AC A0A098Y8A8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:KGH46709.1};
GN ORFNames=IN07_10675 {ECO:0000313|EMBL:KGH46709.1};
OS Modestobacter caceresii.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH46709.1, ECO:0000313|Proteomes:UP000029713};
RN [1] {ECO:0000313|EMBL:KGH46709.1, ECO:0000313|Proteomes:UP000029713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH46709.1,
RC ECO:0000313|Proteomes:UP000029713};
RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT "Biosystematic studies on Modestobacter strains isolated from extreme
RT hyper-arid desert soil and from historic building.";
RL Submitted (JUL-2014) 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:KGH46709.1}.
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DR EMBL; JPMX01000042; KGH46709.1; -; Genomic_DNA.
DR RefSeq; WP_036335644.1; NZ_JPMX01000042.1.
DR AlphaFoldDB; A0A098Y8A8; -.
DR STRING; 1522368.IN07_10675; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000029713; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029713}.
FT DOMAIN 5..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 240..325
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 325 AA; 34912 MW; 21F342C1FC01C970 CRC64;
MHSTHDEVDL RLQVARRTTG AEGVVVLELR DPTGADLPAW SPGAHIDLLL PGGLTRQYSL
CGDPHDRAVW QIGVLREPAG RGGSALVHDQ VQDGTEIDVR GPRNHFELVP AQRYVFLAGG
IGITPILPMA AAAEEAGATW EFHYGGRTRT SMAFLEALEA LEAKTGHGLR VTLHPQDEVG
LIDLDRILGT PQPDTKVYCC GPEPLLAAVE QRCADWPPGS LHVERFAPKE QGERVLSGDF
DVELTLSGTT LTVPPDKSIL QVVEEAGIPV LSSCQEGTCG TCETGVLEGT VDHRDSLLSP
EEQAANDTMF ICVSRAACPK LVLEL
//
