ID A0A0Q7U8Q3_9MICO Unreviewed; 901 AA.
AC A0A0Q7U8Q3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KQZ06012.1};
GN ORFNames=ASD19_12975 {ECO:0000313|EMBL:KQZ06012.1};
OS Microbacterium sp. Root53.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQZ06012.1, ECO:0000313|Proteomes:UP000051407};
RN [1] {ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ06012.1, ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|EMBL:KQZ06012.1,
RC ECO:0000313|Proteomes:UP000051407};
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:KQZ06012.1}.
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DR EMBL; LMFR01000010; KQZ06012.1; -; Genomic_DNA.
DR RefSeq; WP_055988961.1; NZ_LMFR01000010.1.
DR AlphaFoldDB; A0A0Q7U8Q3; -.
DR STRING; 1736553.ASD19_12975; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000051407; 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:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
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; 4.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
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.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051407}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 901 AA; 94611 MW; 3398E66C57E57A79 CRC64;
MRLEIDGAAV EADPRPGQCL RTLLREHGAL SVKRGCDSGD CGACAVLLDG EPVHSCVVPA
VRAEDRAVTT AAGLAPGDAL HPVQDALANG FGFQCGFCTP GMSVTASCLG EEDLPDLDRR
LKGSLCRCTG YRPIREAVRA AVLGPVRETG PDPGDGVGVS AVPEPAQRVV QGLEPYAFDD
VPAGALILRV LGSPHPHARI RAIDAAAARA VPGVVAVYTH EDAPAARYST ARHEHRQDDP
DDTRMLDDVV RHVGQRVAAV VAETAAAAER ACALIRVDYE PLPAVFDPEE ARTPGAPLVH
PERTPEDRVA DAGRNVVAAL HAGYGGDVDA ALAASPVTVS GTWRTGRSIH AQLETHGSVG
WLDEEGRLVI RSSTQVPFLT RDELCTLFDL PRDRVRVYAP RVGGGFGGKQ EMFTEDLVAF
AVLRTGRPVA YEFTRAEQFW RSSMRHPMRV SVTLGAEPDG RLTAIKLDVL SDTGAYGNHA
IGVLFHGCAE SVTLYRAPVA RVDAEAVYTN NVPSGAFRGY GLGQVTLGIE SALDMLAERI
GMDPFDIRRI NAVREGDALR RADGEIEADL VWGSYGLDQC LDLAQAALAE PGEDPPAGWL
VGEGMAAAMI ATLAPRGHRA HATATLLPGG AFELRTGTAE FGNGTTTVQR QIAASVFGVG
ADRIRLAHAD TDAVAFDTGA FASAGTTIAG KALHGACLAL RDRIVEEAAA RVGAPAAECA
YGPDGVRTPA GVVPLAEIAG AGGLTASGEE HGELRSLAFN VHAVRVAVDP ETGAVRILRN
VHAADAGFVM NPAQCRGQIE GGVAQGIGGA LYEEVVVADG RVQNPAFRTY RVPQSADIPD
VEVLFATTSD DLGPFGAKSM SESPYNPVAP AIGNAIARAL GARPFEQPFT RERVWRLAQG
A
//
