ID A0A0P9CAB2_9BACL Unreviewed; 785 AA.
AC A0A0P9CAB2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KPV42347.1};
GN ORFNames=AN477_18090 {ECO:0000313|EMBL:KPV42347.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV42347.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV42347.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV42347.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-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:KPV42347.1}.
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DR EMBL; LJCO01000079; KPV42347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9CAB2; -.
DR STRING; 471514.AN477_18090; -.
DR PATRIC; fig|471514.4.peg.4530; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000050482; 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:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-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:UP000050482}.
FT DOMAIN 18..122
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 766..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 84798 MW; 402CC4C9DCCC0F17 CRC64;
MGAVGQNIPR KDADAKVTGL AKYTDDLSDP GGLHAVLVTS TEGHARILSV DTHDASRAPG
VRAVLTGRDM PVMTGDPIKD RPILAIDTVR YAGEPVAIVI ADELYQAQAG AALVRIAYQP
LPVLQSPRQA FAADAPLIHP NLRDYHWTEE ANPVPGTNIA TKIHIRKGNA HEAFRRCDVV
VECQISFPQS HHAPMETHCA KAKMTVDGHV EITTSTQSPY SNPRVISETF GIRESNVRVE
TPFVGGGFGG KSSTYIEPIV VAAAEAANGK TVQLRCTREQ DMMTVPCHIG LEAVVRLGAT
LDGRLVAAEI SYWFDGGGYS DRGVIVARAA AQDCTGPYRI DHVECHAYCM YTNHPPTTSF
RGFGHPEQTL VMERAMDELA KKLSVDPLEL RRINAILPGD TTPTQARLTR SSIGDVRGCL
NRLQQLLDWQ GPNAIRDGRV VRARGIACVW KTSSTPPNAS SGAIVYVKRD GGVTVVSGIV
EIGQGTKTAL TQIVADVFRI HPDRVDVVFD VNTDEQPEHW KTVASRGSLL AGNAALRAAT
DAVHQLTETA ALAFGCNPQD VRIEDGFAYC PYAENPIPIG DLSHGYVFPD GHTAGSLVVG
RGSYTIEGVT PIDFETGHGV PGPEWTVAAQ GVEVEYRSDD YTYRVIRAVT VVDAGGVLHP
ELALGQVKGA MSMGIGLATR EGYVYDRRGA VTNPQLRVYP MLRYGEQPRY DVEFLTTPHK
DAPYGIRGLG EHGLIGMPAA LANALSNAIG IEVNQMPMTP ELLWRLSQHE DDPKRKRGGV
ARPRG
//
