ID A0A1I7G6Z8_9BACL Unreviewed; 787 AA.
AC A0A1I7G6Z8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=CO or xanthine dehydrogenase, Mo-binding subunit {ECO:0000313|EMBL:SFU44225.1};
GN ORFNames=SAMN05421543_10236 {ECO:0000313|EMBL:SFU44225.1};
OS Alicyclobacillus macrosporangiidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=392015 {ECO:0000313|EMBL:SFU44225.1, ECO:0000313|Proteomes:UP000183508};
RN [1] {ECO:0000313|Proteomes:UP000183508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FPBV01000002; SFU44225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7G6Z8; -.
DR STRING; 392015.SAMN05421543_10236; -.
DR eggNOG; COG1529; Bacteria.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000183508; 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:UP000183508}.
FT DOMAIN 32..141
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 85266 MW; 0B9E8B6BD0594BFF CRC64;
MSKVMEPGVQ SAAPSGQVGR PVKRLESAAK VTGRAEYIHN LELPGMLRAK VVRSTVAHAR
IRGIDTSAAK ALPGVYDVIT AEDILKVIPD PYYGPAFHDQ PILAIDKVRH VGEPVAVVLA
TDVHVADQAT DLVEVEYEEL EPVFHEVEAY KSQTAIVHDV IRPAGTFADL KSLQPRNKTN
VAMEYHLRNG DVDAAFAKAD YVFEHTFRSQ QVNHLPLEPT VTVAQLTDTG NLLIHTSSQS
PSFVRIEVAR LLGWPENKVR VRTAYLGGGF GAKLYIKLEA LVAALALITQ RPVRLSLTME
EQFYTITRHA ATVTIRTGVT KDGRIVARDC KTWWNGGAYA DIGPRVTQKS GFTAAGPYDI
EAVSLDSYAV YTNLPPAGAL RGFGIPQLVW AYESQADIIA RELGMDPLEF RRKNILRNGR
PHATGTILED AGTVEVLEEL ARKMNWDQPF DRGSGTIRRG RGIAIGVKAA VSPTTSVAFV
NLYSDGSCGV YCGTVDMGQG SDTAMAQIAA DVLGLRAEDV RIIHPDTEVT PYDMATLGSR
STFHMGNAVR LAAEDAKQKI VAMCAEQTGF DPAALVVRDG GVATPDGSFF TFGAILAKRH
GMQAGNVLGV GSYFPYYEKP NPETGMSEHI TPYWMVGGTG VEVEVDMETG KVHITRLVTV
GDCGKAINPG IVRRQLSGAS FMQMGFTLFE EMVFDEGQVV NASMADYKIP GFWDLPDINE
VSIVEVPHRN GPFGAKGIGE TGSLGLSPAV ANAIYDAIGV RIYETPLTPE KVLKALREKQ
GQGWEDA
//