ID A0A0Q8QED9_9BURK Unreviewed; 781 AA.
AC A0A0Q8QED9;
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:KRB84195.1};
GN ORFNames=ASE26_08940 {ECO:0000313|EMBL:KRB84195.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB84195.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB84195.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB84195.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB84195.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB84195.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB84195.1}.
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DR EMBL; LMIC01000044; KRB84195.1; -; Genomic_DNA.
DR RefSeq; WP_055924533.1; NZ_LMIC01000044.1.
DR AlphaFoldDB; A0A0Q8QED9; -.
DR Proteomes; UP000051728; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum 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; IPR014309; Xanthine_DH_Mopterin-bd_su.
DR NCBIfam; TIGR02965; xanthine_xdhB; 1.
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:UP000051728}.
FT DOMAIN 34..141
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 781 AA; 84737 MW; 8B60407CACA3711C CRC64;
MNSKSEQFMT LGAAKGWSEV GQSHPHESAI LHVLGEAVYT DDIPEAQGTL HAALGLSTKA
HARIVSLNLE PVKAMPGVVA VYTCKDIPGT NDCGPIIHDD PILAEQKVEY VGQPVFIVVA
DTHDNARRAA RKADIQYEEL PAILTPEAAR DAESFVVPPM RLTRGDAQAA FERSPNILEG
KLHVGGQEQF YLEGQISYAV PKEGKGMHVY CSTQHPTEMQ HVVSHALNYP SHAVVVECRR
MGGGFGGKES QSALWAACAA VSAARLKRPV KLRADRDDDM MVTGKRHCFY YEYEIGYDHQ
GLITAAKVQM VTRAGFSADL SAPVATRAIC HFDNTYYLSD VDIRAMAGKT NTQSNTAFRG
FGGPQGAIAI EYIIDEIARN LGKDALDVRK LNFYGRNDEE GRNVTQYGQK VVDNVIHELV
AQLESDTKYR SRREAVHKFN ASNPVLKKGL ALTPVKFGIA FNVTHFNQAG ALVHIYVDGS
VLVNHGGTEM GQGINTKVCL VVAHELGIPL SSVRASATDT SKVANTSATA ASTGADLNGK
AAQDAAHTLR RRLVEFAAKS FGVTAEEVIL ANGTVFAGET VIPFADLVQK AYLARVQLWS
DGFYATPGLS WDRETMSGNP FGYYAYGASV SEVIVDTLTG EWKLLKADCL YDAGNSLNPA
IDVGQVEGAF MQGMGWLTTE ELWWNQQGKL MTHAPSTYKI PGVSDCPEDF NVRLFRNRNP
FDSIHRSKAV GEPPLLLPFS VFLAIRDAVA SVGNYRINPP LRAPATGEAI LDAVDAVRAQ
A
//
