ID   A0A0J7AEY8_9ACTN        Unreviewed;       801 AA.
AC   A0A0J7AEY8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KMO95776.1};
GN   ORFNames=ACS04_21360 {ECO:0000313|EMBL:KMO95776.1};
OS   Streptomyces roseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO95776.1, ECO:0000313|Proteomes:UP000035932};
RN   [1] {ECO:0000313|EMBL:KMO95776.1, ECO:0000313|Proteomes:UP000035932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO95776.1,
RC   ECO:0000313|Proteomes:UP000035932};
RA   Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA   Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA   Barona-Gomez F.;
RT   "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT   hidden chemical diversity on bacterial genomes.";
RL   Submitted (JUN-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:KMO95776.1}.
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DR   EMBL; LFML01000085; KMO95776.1; -; Genomic_DNA.
DR   RefSeq; WP_048478301.1; NZ_LFML01000085.1.
DR   AlphaFoldDB; A0A0J7AEY8; -.
DR   STRING; 66430.ACS04_21360; -.
DR   PATRIC; fig|66430.4.peg.7121; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000035932; 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   InterPro; IPR017609; Xanthine_dehydrogenase_dsu.
DR   NCBIfam; TIGR03196; pucD; 1.
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:UP000035932}.
FT   DOMAIN          39..146
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  85283 MW;  F205CF97827EDEBC CRC64;
     MAQNTRTVPA GTPTNVTQKH NKGGIGESTL RPDGTLKVTG EFAYSSDMWH EDMLWGQTLR
     STVAHAEIAS IDISEALAMP GVYSVLTYDD LPAAMKNYGL EIQDTPVLAN GRVRHHGEPV
     ALVAADHPET ARRAAAKIKI DYRELPLVTD EASALAPDAP LIHPGRDDHH SGHVPHPNIV
     HRQPIIRGNV EEARKRADVI VEGEYTFGMQ DQAFLGPESG LAVPSEDGGV DLYVATQWLH
     SDLKQIAPVL GLPEEKVRMT LSGVGGAFGG REDISMQIHA CLLALATNKP VKIVYNRFES
     FFGHVHRHPA KLYYEHGATK DGKLTHMKCK IVLDGGAYAS ASPAVVGNAS SLSVGPYVLE
     DVDIEAIALY TNNPPCGAMR GFGAVQACFA YEAQMDKLAA KLGMDPVEFR QLNAMEMGTI
     MPTGQVVDSP APVAELLRRV KSRPLPPERQ WESAGEGADV RALPGGLSNT THGEGVVRGV
     GYAVGIKNVG FSEGFDDYST ARVRLEVING EPVAMVHTAM AEVGQGGVTV HAQIARTELG
     VTQVTIHPAD TQVGSAGSTS ASRQTYMTGG AVKNTCEAVR EAVLEIGRRK NGSYHPAWAT
     AELLLEGGKI VTDGGEVLAD IADVLEGEDA IDLELEFRHR PTVAFDLKTG QGDGHVQYTF
     AAHRAVVEVD TELGLVKVVE LATAQDVGKA LNMLSVVGQI QGGTTQGLGV AIMEEIIVDP
     KTAKVRNPSF TDYLIPTILD TPTIPVDVLE LADPNAPYGL RGMGEAPTLS STPAVLAAIR
     AATGLELNKT PIRPEALTGT L
//