ID A0A1G5L0W1_9ACTN Unreviewed; 778 AA.
AC A0A1G5L0W1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=CO or xanthine dehydrogenase, Mo-binding subunit {ECO:0000313|EMBL:SCZ06583.1};
GN ORFNames=SAMN02745898_10869 {ECO:0000313|EMBL:SCZ06583.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCZ06583.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCZ06583.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCZ06583.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMVI01000008; SCZ06583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5L0W1; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000199326; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000199326}.
FT DOMAIN 47..153
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 81511 MW; F1ADC7410A401F6F CRC64;
MSNDAATAAN ATRTTLTTPP VDSPDTEPPV FGIGASLPPA DARAKTEGTF PYAADLWAEG
LLWAAVLRSP HPHARILSID TSAAAEMPGV RTVVTHEDVP GDGAYGRRVV DRPVFASELV
RHHGEPIAAV AADHPDTARL AAAAIVVEYE ILEPVTDPEK AFEAEPLHPD GNLIRHIPLR
YGDPDIAGEV IVEGLYRIGR QDPAPIGAEA GLAVPRPDGG VEIYTASTDP HTDRDLAAAC
FGLEPDRVKI VVTGVPGATG DREDPGFQLP LGLLALRTGC PVKLAATREE SFLGHAHRHP
TLLRYRHHAD AEGRLVKVEA QILLDAGAYA DASSESLAAA VAFACGPYVV PHAFIEGWAV
RTNNPPSGHV RGEGAMQVCA AYEGQMDKLA AKLGIEPAEL RLRNSLSTGD ILPTGQTVTC
PAPVAELLRA VRDFPLPTLP KDSPEDDWLL PGGPEGAGEP GAVRRGVGYA LGMVHMLGAE
GADEVSTATV KVHDGVATVI CAAVETGQGF STLARQVVQE TLGIEEVHVA SVDTDQPPAG
PATHGRHTWV SAGAVERAAK MVRTQLLQPL AHKFGMSTEL LQIANGKITS YDGVLSTTVT
EAMDGKELWA TAQCRPHPTE PLDESGQGDA FVGLAFCAVR AVVDVDIELG SIRVVEMAVA
QDVGRVLNPS QLATRIEAGI TQGIGTALTE NLRTARGLIR HPDLTGYALP TALDAPDIRI
VKLVEERDVV APFGAKPASA VPVVTSPAAV AAAVRAATGR PINRLPIRPQ AAVAAVNS
//