ID A0A1B6AKU3_9ACTN Unreviewed; 718 AA.
AC A0A1B6AKU3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aldehyde oxidoreductase {ECO:0000313|EMBL:GAU67964.1};
GN ORFNames=SSP35_06_00470 {ECO:0000313|EMBL:GAU67964.1};
OS Streptomyces sp. NBRC 110611.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU67964.1, ECO:0000313|Proteomes:UP000094479};
RN [1] {ECO:0000313|EMBL:GAU67964.1, ECO:0000313|Proteomes:UP000094479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU67964.1,
RC ECO:0000313|Proteomes:UP000094479};
RA Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:GAU67964.1}.
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DR EMBL; BBUY01000006; GAU67964.1; -; Genomic_DNA.
DR RefSeq; WP_066931546.1; NZ_BBUY01000006.1.
DR AlphaFoldDB; A0A1B6AKU3; -.
DR STRING; 1621259.GCA_001590865_03260; -.
DR OrthoDB; 159930at2; -.
DR Proteomes; UP000094479; 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 CDD; cd00207; fer2; 1.
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:UP000094479}.
FT DOMAIN 513..590
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 71932 MW; E1826E234F1AF63A CRC64;
MSDADSRHPQ QQPADQGWQP LPQGGEYEQE ATAFVQLPEG FTTGVYGGRA PDRAPGADPL
AAPGHGYTPP ASFTPQPPAP PVAGTDPAAT GQWTMPFADP SAGYADPSAG YAAPTSAHTD
GTAHHDPSTG YQGGAPGGAQ PWGGGAPVQW PEAGGPQTGA PYPGGGTWSV PAAADDGLEE
SGEYRVGGYQ DGGYPHAGAY RGADAGTSDG TDPDAAARTG HWNFTTGLSA THLRETRSTE
PQEASRGAAD EVPFGAPADG SYAPESGFPG RGTAPVEDHR PAPAPEPAPG GPDAMAGGAT
GHWSLPADAL AQWPPATETA RPAHDGASDV PAPAGAAGWT AAPAPTAPVN PTAPIADGER
LPDSAELPPS GEFTAPDEAE QTEAEAEVEA EDAADASSAD TPATPDTPDT PQPDTRPEAV
VPAESAPESA PETAPGELAD HDDGTDGTDG TDGSTDRAET AEAAEAAEGA EATGATEGDD
GTDPLSTDTL NKGAEAPAAP HGEHHEHNEH PAASYVLRVN GIDRPVTDAW IGESLLYVLR
ERLGLAGAKD GCSQGECGAC SVQVDGRLVA SCLVPAATAA GSEVRTVEGL ARNGAPSDVQ
CALAASGAVQ CGFCVPGMAM TVHDLLEGNP APSELETRKA LCGNLCRCSG YRGVLDAVEE
VVKARAEAAE AAEAAPSAED GPAVAPPPDT ARIPHQAGPA DPMGRAPHDQ DPHTGGTA
//
