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Database: UniProt
Entry: A0A1Q5MD47_9ACTN
LinkDB: A0A1Q5MD47_9ACTN
Original site: A0A1Q5MD47_9ACTN 
ID   A0A1Q5MD47_9ACTN        Unreviewed;       562 AA.
AC   A0A1Q5MD47;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:OKK11975.1};
GN   ORFNames=AMK09_30415 {ECO:0000313|EMBL:OKK11975.1};
OS   Streptomyces sp. CB02488.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK11975.1, ECO:0000313|Proteomes:UP000186200};
RN   [1] {ECO:0000313|EMBL:OKK11975.1, ECO:0000313|Proteomes:UP000186200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02488 {ECO:0000313|EMBL:OKK11975.1,
RC   ECO:0000313|Proteomes:UP000186200};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKK11975.1}.
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DR   EMBL; LIVO01000016; OKK11975.1; -; Genomic_DNA.
DR   RefSeq; WP_073738182.1; NZ_LIVO01000016.1.
DR   AlphaFoldDB; A0A1Q5MD47; -.
DR   STRING; 1703920.AMK09_30415; -.
DR   OrthoDB; 159930at2; -.
DR   Proteomes; UP000186200; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
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   PANTHER; PTHR44379; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR44379:SF8; XANTHINE DEHYDROGENASE IRON-SULFUR-BINDING SUBUNIT XDHC-RELATED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186200}.
FT   DOMAIN          359..436
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   REGION          1..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..214
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  57852 MW;  13FE3B68BC8C715A CRC64;
     MSNEDHTEQH GGWEPIPQSG EYDGESTAFV HLPPEDLANI PLAAPGQGYV PPMILPLTPA
     AGIDPAATGS WVVRTPDGQD SRGDGQDHAP GAEQPAPEAV HWPDPNQQQA PYGYQQTPYQ
     PHPPAEQYPD RYREDRAATG QWNFAESAES AEPAGHTGQW QIPVADGDLP EESGEFSPSA
     AAAWYADRTP PATLPGGAPA PWATREPEPP AGDSAPPQGA DHDGTPDAPD GAADAHEVPP
     EAALQDASQP AMEHPGPAEP VTEPGTEPVA EPAADPVAEP VAEDAPDTGA TDAETAPDTD
     VTAPDATDTP AEADATDPGV TEHAPTPDLA PDLDADPDVT DPEAAPAPRL DLPSEHPSVS
     YALHVNGVDR PVTGAWIGES LLYVLRERLG LAGAKDGCSQ GECGACNVQV DGRLVASCLV
     PAATAAGSEV RTVEGLAVDG EPSDVQRALA DCGAVQCGFC IPGMAMTVHD LLEGNHAPSE
     LETRQALCGN LCRCSGYRGV LDAVNEVIAG REAASAPAPE SAEQSTGQST EQSAKQDEAR
     IPHQAPPGAG SVQAHLQDGG MA
//
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