ID   A0A3A5HF19_9ACTN        Unreviewed;       862 AA.
AC   A0A3A5HF19;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:RJS46580.1};
GN   ORFNames=D4739_10385 {ECO:0000313|EMBL:RJS46580.1};
OS   Nocardioides cavernaquae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2321396 {ECO:0000313|EMBL:RJS46580.1, ECO:0000313|Proteomes:UP000276542};
RN   [1] {ECO:0000313|Proteomes:UP000276542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1W22B-1 {ECO:0000313|Proteomes:UP000276542};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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:RJS46580.1}.
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DR   EMBL; QYRP01000002; RJS46580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5HF19; -.
DR   OrthoDB; 9758509at2; -.
DR   Proteomes; UP000276542; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276542}.
FT   DOMAIN          1..72
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   862 AA;  90664 MW;  AF570FD57068E3ED CRC64;
     MRINGSSVTT DPRPGQCLRT YLREQGDTAV KKGCDAGDCG ACSVLLDGRP VHSCITPAVR
     AIGHEVTTAA GLAPEGALCA TQQCFVDGAG FQCGYCTAGF VVTAHGSGHA PHSTDLERTF
     KGNYCRCTGY RAIRDSLAGS VNVGGSTFGD PVGAPAGRRI VAGREPFTLD LPEAGVLHAK
     ALRSPHPHAR IIAIDTVRAE ALDGVHLVLT HRDSPSMHFS TARHESRLDD PDDTLVLDPV
     VRFAGQRVAV VVADSVAIAT RALDLIDVTY EQLPAVFDPE AARLPGAPLL HGEKDPVVAR
     ISDPARNVVA QTHGEVGDVA AGLATAAATV SGRWTTSPVT HASLETHGAR AWLDDDGRLV
     VRTSSQVPFL VRDELAQLLG LPADQVRVLT TRVGGGFGGK QELLVEDVVA LATLRLRRPV
     QWELTREEQF TAIPWRHPFI VDLTLGADAD GVLTAMALDV VSDTGAYGNH AVGVLFHGCH
     ESVAQYRCPN KRVDAEAVYT NNPPSGAFRG YGLGQVMWAV ESALDDLARE IGISAAEIRR
     RNVVTPGDEF VVNAHAPDDL QYGSYGLDQC LDLVEAALAS GEGDTAPEGW SVGEGLAVAM
     IATIPPRGHH ATASVTAESD GSFTVQAGSA EFGNGTATVH VQLAAEALGV PTGRVRLVAG
     DTDAAAYDTG AFGSAGSAVA GLAVQRAATS LRRAIDDGAD LPLTAFGEHD GTPRSVAFNV
     HGFRVAVDPA TGSVRVLTSV QAVDAGVIIN PEQLRGQVEG GIAQAIGSAL QEELVVRDGQ
     VLTRTFRNYR FPQIADVPPT RILYADTFDP LGPSGSKSMS EAPYNPVAPA LANAIRDAAG
     VRARHLPMSR DRVWRLIREE SR
//