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Database: UniProt
Entry: A0A1Q5ITN7_9ACTN
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Original site: A0A1Q5ITN7_9ACTN 
ID   A0A1Q5ITN7_9ACTN        Unreviewed;       799 AA.
AC   A0A1Q5ITN7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:OKJ60464.1};
GN   ORFNames=AMK29_24820 {ECO:0000313|EMBL:OKJ60464.1};
OS   Streptomyces sp. CB02261.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ60464.1, ECO:0000313|Proteomes:UP000186742};
RN   [1] {ECO:0000313|EMBL:OKJ60464.1, ECO:0000313|Proteomes:UP000186742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02261 {ECO:0000313|EMBL:OKJ60464.1,
RC   ECO:0000313|Proteomes:UP000186742};
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:OKJ60464.1}.
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DR   EMBL; LIVX01000008; OKJ60464.1; -; Genomic_DNA.
DR   RefSeq; WP_073817289.1; NZ_LIVX01000008.1.
DR   AlphaFoldDB; A0A1Q5ITN7; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000186742; 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.
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; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11908:SF157; XANTHINE DEHYDROGENASE SUBUNIT D-RELATED; 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;
FT   DOMAIN          39..145
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  85073 MW;  5AC15CBEF7909EA2 CRC64;
     MAQNTRTVPA GTPTDVTQKH VKGGVGESTL RPDGTLKVTG EFAYSSDMWH EDMLWGQILR
     STVAHAEIVS IDTSEALTMD GVYAVLTHED LPAAKNYGME FQDTPVLAYG KVRHHGEPVA
     LVAADHPETA RRAAAKIKVE YRELPLITDE ASATAPDAIL VHEGRDDHHS GHVPHPNIVH
     RQPIIRGNAD EAAKRADVIV RGEYTFGMQD QAFLGPESGL AVPAEDGGVD LYVATQWLHS
     DLKQIAPCLG LPEEKIRMTM AGVGGAFGGR EDISMQILAS LLALRTGKPV KMVYNRYESF
     FGHVHRHPAK LWYEHGATKD GKLTHLKCKI VLDGGAYASS TASVVGNAAS LSVGPYVVDD
     VEIEAVGLYT NNPPCGAMRG FGAVQACFAY EAQMDKVAAK LGMDPVEFRQ INAMEQGTIM
     PTGQLVDSPA PVAELLRLVK ARPMPPERQW ETAGEGADVR ALPGGLSNTS HGEGVVRGVG
     YAVGIKNVGF SEGFDDYSTA RIRMEVINGE PVATVHTAAA EVGQGGVTIH AQIARTELGV
     QQVTIQPADT QVGSAGSTSA GRQTYMTGGA IKNSCELVRE KVLEIGRRKF GSYHPAWATA
     ELLLEGGKVV TDGGEALATI ADVLEDQAVE VEEEWRHRPT QAFDLVTGQG NGHVQYAFAA
     HRAVVEVDTE LGLVKVIELA CAQDVGKAVN PLSVVGQIQG GTTQGLGVAV MEEIIVDPKT
     AKVRNPSFTD YLIPTILDTP TIPVDYLELA DPNAPYGVRG IGEAPTLSST PAVLAAIRAA
     TGLELNKTPV RPEALTGTL
//
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