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
//