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Database: UniProt
Entry: A0A0Q6F849_9ACTN
LinkDB: A0A0Q6F849_9ACTN
Original site: A0A0Q6F849_9ACTN 
ID   A0A0Q6F849_9ACTN        Unreviewed;       896 AA.
AC   A0A0Q6F849;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KQT90729.1};
GN   ORFNames=ASG49_13335 {ECO:0000313|EMBL:KQT90729.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT90729.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT90729.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90729.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT90729.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90729.1,
RC   ECO:0000313|Proteomes:UP000051542};
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   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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:KQT90729.1}.
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DR   EMBL; LMRF01000005; KQT90729.1; -; Genomic_DNA.
DR   RefSeq; WP_056542661.1; NZ_LMRF01000005.1.
DR   AlphaFoldDB; A0A0Q6F849; -.
DR   STRING; 1736379.ASG49_13335; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000051542; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
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; 5.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
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; IPR012675; Beta-grasp_dom_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; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 2.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT   DOMAIN          188..300
FT                   /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT                   hammerhead"
FT                   /evidence="ECO:0000259|SMART:SM01008"
SQ   SEQUENCE   896 AA;  94410 MW;  C989B14F84220C4D CRC64;
     MTDLDQRPPG GTPVAAATRV NGAELAGEPA AGQCLRTWLR QHDHLEVKKG CDAGDCGACT
     VLLDGRPVHS CVVPAVRAVG REVTTAAGLG TPEDLHPVQR RFVDAQGFQC GFCTAGFVTT
     AAALADAEGR VGEDPERLAR DFKGNLCRCT GYRSIRDALA GRTNVEAAPA VGGFGCSVGA
     PAGPRLATGR EAFTLDQPGT GVLHMALLQS PRAHARITRL DTAAAEALPG VHLVLTHRDV
     PDVRYSTARH ESRTDDPDDT RMLDDVVRFR GQRVAAVVAD DLVTASRALD LLVVEYADLP
     VVLDPEQARL PGAPLLHPDL DPVTSRVSDP GRNVVAQTHG EVGDVAGALA ASAVRVGGTW
     RTGRVNQAAL ETHGARGWLD ERGVLVVRSS TQVPFLVRDE LAHVFGIRPE LVRVVAARVG
     GGFGGKQEML VEDLVGLAVL RLGAPVQLEL TREQQFTLVP GRHPMRVSVE LGADADGVLS
     AMRVDVLTDT GAYGNHAPGV MFHGCHESIA LYRCANKRLD AEAVYTNHVP SGAFRGYGLG
     QVVFAIESAL DELAREVGIS PFDVRRRNVV VPEDHFVVNG PPDTDLVFGS YGLDECLDLV
     EASLERDDLP PPPPGWAVGR GMAASMIATI PPRGHHAEAT VTMHPDRSVV VAVGSAEFGN
     GTATVHTQIA AAELDVPVSA VSLVTSDTAR TGYDTGAYGS TGSVVAGRAV AHAARSLRSL
     LDPMEGPLVG PVSATGRHHG SPRSVAFNVH GFVVAVDPGT GEVRVLHSVQ AADAGVVINP
     EQLRGQVEGG VAQGIGSALY EEVVVDDGPG GDGHVTSRVL RDYRLPQIGD VPATEVLLAD
     TYDELGVRGA KSMSEAPYNP VAPALANAVR DALGVRPHEL PMSRDRLWRL MQEERS
//
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