ID A0A124GZV6_9ACTN Unreviewed; 900 AA.
AC A0A124GZV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KUM73441.1};
GN ORFNames=AQI70_22000 {ECO:0000313|EMBL:KUM73441.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM73441.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM73441.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM73441.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-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:KUM73441.1}.
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DR EMBL; LMWJ01000015; KUM73441.1; -; Genomic_DNA.
DR RefSeq; WP_062152709.1; NZ_KQ947989.1.
DR AlphaFoldDB; A0A124GZV6; -.
DR STRING; 146536.AQI70_22000; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000054024; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024}.
FT DOMAIN 168..281
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 900 AA; 96212 MW; BDA9B496DC097A6F CRC64;
MAFLTRINGR DSHEPPAPGQ CLRTYLRQQG WFGVKKGCDT GDCGACTVHV DGVPVHSCLY
PAHRAHGRTV TTVEGLATDG QLQPVQRAFL NAHAFQCGYC TPGFVMTAAA LTPTQLRALP
ESLKGNLCRC TGYRVIEEAV RDAHRPQAAA TGAASRDEDA SADAAVVCGI APFTLDTPAP
TGMLHIRLVR SPHRHARITA IDTEAAQAMP GVHAVLTHQD APAVRFSTAL QERTSDNPAD
TRLLDDVVRH VGQRVAVVVA DSPAAAEDAC RRVRVTYDVL PAVTDPDQAL RAGATRVHPS
GNLAHRLHTV VGDIELGLAQ ADAVHTQTYK THRVQHTALE CHATRAWRDE DGRLHVHTTT
QSPHLTRRHL CAVFGLQPHQ VQVTAARLGG AFGGKQEMLT EDIAVLAVLR TGRPVQLEYT
RTEELTATTT RHPFHVTVTA GARRDGTLTA LKVRVVADTG AYGNHGPAVL QVACAEALSL
YRCANITVDG YSVYTHNVPS GAFRGYGIGQ MAFAVESALD ELAHTLALDP LTLREHAYLR
PGETSPLADG DQPAPTADTG LTDVLRTLRT VRDRRPPPSS AAVDARCLIG QGLAVTAQST
HPSDGHITQV IAQLRPDGDY DLITGPPEFG TRATDLLRHT AATALATSPG HIHFRCADTD
LLDHDTGGFA STGATLGTQA VQRACRQLRE QLLALAADRT GADAAACRLE GDVVHCGDRR
LPLNELHATA RHEGEPLRAI GRAEPCTGPS PLAVNAHWFR IAVHPETGAL TILDSVHVAD
AGTVLNEASC NGQIHGAIAQ GIGTTLWENL STEPDGRITT QDLRSYTIPQ LADIPDTEIH
FCRPTTPDRG PKPLGEGPFN PIAPALANAL RDATGIRFTT LPLRADMVWA ALHQHRGGQL
//
