ID M7A1T8_9ACTN Unreviewed; 928 AA.
AC M7A1T8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:EMP12653.2};
GN ORFNames=ISGA_1682 {ECO:0000313|EMBL:EMP12653.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP12653.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP12653.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP12653.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP12653.2}.
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DR EMBL; APHK02000076; EMP12653.2; -; Genomic_DNA.
DR RefSeq; WP_053777880.1; NZ_APHK02000076.1.
DR AlphaFoldDB; M7A1T8; -.
DR STRING; 1241906.ISGA_1682; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000011989; 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:UP000011989}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 928 AA; 97986 MW; A1506E5720FA28E2 CRC64;
MRFEINAESV DAEPRPGQCL RTFLRDTGHF EVKKGCDAGD CGACSVLVDG VPVHSCIYPA
QRIDGASVTT VAGLGTPDDL HPMQQSFVDN FGFQCGFCTA GMIVTASTLT PDDLDDLPRR
MKGNLCRCTG YRAIRAAITA GVTGTPAPTP PTCAALCGTT GDAGATGTPV GTSINPLAAR
RVVTGTEPYT FDVDVPGTQY LRVLTSPHPH ARITRIDTTE AAAVDGVNLV LTHENVSTPR
FSTGRHESRL DDPDDTLILD PVVRFVGQRV AAVVADTAAA AEQACRLIEV DYETLPAVFD
PVEARRPGAA LVHPDRTPAD RVAAADRNVI AEFHEGFGGD VDEALATAAV TVGGSWQTAR
VSHAQLETHG SIGWLEDDRL VIRTSTQVPF LVRDELARLL DLPAERIRVF AARVGGGFGG
KQELLTEDLV AVAVLRTGRP VAYEMTRTDE MTRTTYRHPF RVAVDLGADA DGRLTAMKVD
VLSDTGAYGN HAIGVMFHAC AESVSVYNCP VKRVDAEVVY TNNPPSGAFR GYGLGQVIFA
VESAMDELAI RLGIDPFDLR RINAVAEGDP LLIAHEEPEE DLVYGSYGLD QCLDLAQSAL
ARGGGDAVPD GDHWRIGEGM ALAAIATMAP RGHFSTVTVG VDAAGIYHVG VGTCEFGNGT
TTVHAQIAAS ALSTEIENIR VSHGDTDAAP YDTGAFASAG TTVAGKAVHG AALALRQTLI
AAAPSLTGST PDRVRLGSDG AAVGDRMLGF GELIAAVDED HRQDHPDGAR AVASGSERGD
LRSIAFNVQG FRVAVNTETG AVRILQSVHA ADAGTVMNPQ QCLGQVEGGV AQAIGAALYE
EIMLDGKGVP LTPVFRTYRV PQMADIPDTE VYFADTSDDL GPYGAKSMSE SPYNPVAPAL
ANAIRRAIDA RPYETPMSRD RVWRLAQG
//
