ID A0A0L1LP37_9MICC Unreviewed; 951 AA.
AC A0A0L1LP37;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KNH18065.1};
GN ORFNames=ACU18_08725 {ECO:0000313|EMBL:KNH18065.1};
OS Arthrobacter sp. ZBG10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1676590 {ECO:0000313|EMBL:KNH18065.1, ECO:0000313|Proteomes:UP000036861};
RN [1] {ECO:0000313|EMBL:KNH18065.1, ECO:0000313|Proteomes:UP000036861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZBG10 {ECO:0000313|EMBL:KNH18065.1,
RC ECO:0000313|Proteomes:UP000036861};
RA Hoefler B.C., Straight P.D.;
RL Submitted (JUN-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:KNH18065.1}.
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DR EMBL; LFQH01000033; KNH18065.1; -; Genomic_DNA.
DR RefSeq; WP_050685142.1; NZ_LFQH01000033.1.
DR AlphaFoldDB; A0A0L1LP37; -.
DR PATRIC; fig|1676590.3.peg.1577; -.
DR Proteomes; UP000036861; 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 PIRSF; PIRSF000127; Xanthine_DH; 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.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 99735 MW; 66413B2578E07FFA CRC64;
MAISINGTAA DAAPRPGQCL RTFLREQGNS GVKKGCDGGD CGACTVHVDG TPVHSCIYPA
VRAEGHAVTT IEGLAATAAE PSESGLHPVQ QQFMERQGFQ CGFCTAGMLM TAATFDAEQE
SNLPRSLKGN LCRCTGYRAI GDAICGHAGH PAPEGPGSGI AGDSQPDPVP GQLGDDVPAP
ASRAVVTGAA RYTLDLPVAE QQALLHLKIL RSPHASARVL SVDAAAALEI PGVVAVLTSA
DAPEQLFSTA QHELFTDDPD DTRVLDDVVR FIGQRVAAVV AETVAAAEAG VRALAVDYEV
LPAVFSPQDA LQPGAPQVHG DKDGPIARIS RPDRNVVAEL HSELGSVADG FAAADFIHEQ
TYRTQRVQHV ALETHAAIAS VDPAGRIQIR TSSQVPFLVR RTLCRIFGLP EDGVHVVAGR
VGGGFGGKQE VLTEDLVALA ALKLGRPVQL ELTRTEQFTA TTTRHPFTIA LKAGASADGR
LTALELDVVT NTGAYGNHGP GVMFHGCGES LSVYKCANKK VDAHSVYTNT VPAGAFRGYG
LSQMIFAIES AMDELATGIG MDPQEFRRRN MVRKGDDMLS TQPEPEEDVH YGSYGLDQCL
DLVRDALQRG QDRYREAGLD DLGPDWLVGE GQALSMIDTV PPRGHFAHSK IRLLPDGTYQ
ADVGTAEFGN GTTTVHAQLA ATALATESTR VQVRQSDTDL IEHDTGAFGS AGTVVAGKAT
LAAAEELAVR IRAFAAGIRQ TQASACVIHG ATVVCDGTDV PLTELAAAAA EAGVELAAEG
RWGGTPRSVA FNVHGFRVAV NRNTGELKIL QSVQAADAGV VVNPRQCRGQ IEGGIAQAIG
ATLYEEVVVD DAGRVTTDIL RQYHIPTFAD VPRSEVYFAD TNDSTGPLGA KSMSESPFNP
VAPALANAIR NATGVRFAQL PIARDRIYLG LREAGKVPAA EAGVGQGHLV S
//
