ID A0A0P7G6Z9_9MICC Unreviewed; 921 AA.
AC A0A0P7G6Z9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:KPN16277.1};
GN ORFNames=AO716_15430 {ECO:0000313|EMBL:KPN16277.1};
OS Arthrobacter sp. Edens01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN16277.1, ECO:0000313|Proteomes:UP000054460};
RN [1] {ECO:0000313|EMBL:KPN16277.1, ECO:0000313|Proteomes:UP000054460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edens01 {ECO:0000313|EMBL:KPN16277.1,
RC ECO:0000313|Proteomes:UP000054460};
RA Couger M.B.;
RT "Draft Genome of Arthrobacter sp. strain Edens01.";
RL Submitted (SEP-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:KPN16277.1}.
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DR EMBL; LKIU01000006; KPN16277.1; -; Genomic_DNA.
DR RefSeq; WP_055242484.1; NZ_LKIU01000006.1.
DR AlphaFoldDB; A0A0P7G6Z9; -.
DR STRING; 1732020.AO716_15430; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000054460; 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:UP000054460}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 921 AA; 96349 MW; ABD3BA867710C8BA CRC64;
MSYTVNGRPT DAEPAPGQCL RTFLRELGNT GVKKGCDAGD CGACTVHVDG MPVHSCIYPA
RRADGRDVTT IEGLADGGIL HPMQQQFLAA QGFQCGFCTA GMIMTAAAFG PADRADLPRA
LKGNLCRCTG YRAVEDAVAG TQRVDDGGSG VGESVPAPAG PAIVTGAARY TLDVPPGTYP
DLLHLALARS PHAHARIVSI DAAAALAVPG VEAVFTHEDA PALRFSSAQH ELHTDDPADT
RVLDDVVRFK GQRVAVVAAA SVAAAEAGVR ALRIDYEILP AVFEPDEALA PGAPLLHEAA
AAEPGVGTPA PSNIVAELHA ELGNPEAGFA AAVAVHEGTY YSQRLQHVAL ETHAAIASFD
EHGRLVVRTS TQVPFLVRRT LCRVFDLQLE KVRVVSGRVG GGFGGKQEVL VEDVAVLAAL
RLGRQVQIEL SREEQFTAST TRHPFRVRVK AGADAQGMLT ALAVDVTTNT GAYGNHGPGV
MFHGCGESVA VYRCANKKVD ARAVYTNTVP AGAFRGYGLS QMIFAIESAL DELARTLDLD
PLEFKRRNLV VEGDPMLSTS PEAAGDVLYG SYGLDECVDL VRGALKDGAK DPLRSGGDLG
PGWLVGEGTA VAMIDTVPPR GHVAHTRIAL RPDGRYGLDV GTAEFGNGTT TVHTQLACTA
LATLPQNVVI RQSDTDLVDH DTGAYGSTGT VVAGKATLAA AAELATKLQG FAASLFRNTS
AQVSLEADAV ACGDERVPLA EVYLRAAEAG VELAAEGRWG GTPRSVAFNV QGFRVAVDPS
TGEIRILQSV QAADAGVVVN PLQCRGQIEG GVAQAIGAAL FEEVLVDRSG EVQTRVLRQY
HVPAFADVPR TEVLFASTSD SLGPLGAKSM SESPFNPVVP ALANALRDAT GLRFTRPPFA
RDRVYLALRG AGVPARPLTV Q
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