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Database: UniProt
Entry: A0A0Q6L305_9SPHN
LinkDB: A0A0Q6L305_9SPHN
Original site: A0A0Q6L305_9SPHN 
ID   A0A0Q6L305_9SPHN        Unreviewed;       777 AA.
AC   A0A0Q6L305;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQU61950.1};
GN   ORFNames=ASG67_01990 {ECO:0000313|EMBL:KQU61950.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU61950.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU61950.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61950.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU61950.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61950.1,
RC   ECO:0000313|Proteomes:UP000051371};
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:KQU61950.1}.
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DR   EMBL; LMRS01000001; KQU61950.1; -; Genomic_DNA.
DR   RefSeq; WP_056524516.1; NZ_LMRS01000001.1.
DR   AlphaFoldDB; A0A0Q6L305; -.
DR   STRING; 1736343.ASG67_01990; -.
DR   OrthoDB; 8428274at2; -.
DR   Proteomes; UP000051371; 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.
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:UP000051371}.
FT   DOMAIN          61..175
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
SQ   SEQUENCE   777 AA;  81929 MW;  32B1186C81C0D8C7 CRC64;
     MSILDTAKEA AQGLVQGAMA KLVPLAPDSW IPGGVPDPLI ARKHGLIGTS VPRLDGPLKV
     KGAARFAAEF ALDDMVYAAL AFATIPRGRI ATLDVAAAEA ASGVVAVMTH RNAPRMKQPA
     VFGSSPTAAG PADLPIMQDD RIHWNGQPIA VVLAETQEQA DHAVSLIVAT YEVEEAVTSF
     AAAKEKGAAP ASFMGQPLVN EIGDADAMLA AAPHKVDHVY RTPRHNHNAI EPHAATIAWV
     GGDLVVHDAS QLVSMEAATI AGVFDLNVEQ VRVTSPYVGG GFGGKCLWDH QILGAAAAKL
     AGRPVRIALT REGVYRGVGG RTLTEQRVAI GAAADGHFQA LIHAGTTATT PHNNMPEPFI
     LGTRAGYAAD SIKLSVDVVR MNMLANTFMR APGESVGTFA LESAIDELAV DLGIDPIELR
     ICNEPDVDPT SGLPFSARHI VEAWRAGAEK FGWDKRELPG AQREGEWLIG MGCATGTYPY
     YRMPGAAARI TLDRAGTALV EVAAHEMGMG TSTTTTMVAA DRLGLPLEAV EVRYGDSIIP
     GAILAGGSQQ TAAIGAAVIA AHNALVAELL KLAGNDSPLA GLSPDEVGSE DGGLAKLDDP
     ARRESYASIL QRAQRDQVSV SAEGSMPLEL MHWSMHSHSA IFCEVRVNAV TREIRVSRFL
     GSFDCGRILN PKTARSQFRG GMIMGLGLAL MEETEFDERN GRIMNPSLAE YHMPVHLDVP
     EIEVIWTDIA DPHTPMGAHG VGEIGITGVA AAVANAVYNA TGTRVRDLPI TLDKLLV
//
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