ID A0A1E8Q1S8_9MYCO Unreviewed; 882 AA.
AC A0A1E8Q1S8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:OFJ52492.1};
GN ORFNames=BEL07_17345 {ECO:0000313|EMBL:OFJ52492.1};
OS Mycobacterium grossiae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1552759 {ECO:0000313|EMBL:OFJ52492.1, ECO:0000313|Proteomes:UP000178953};
RN [1] {ECO:0000313|EMBL:OFJ52492.1, ECO:0000313|Proteomes:UP000178953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCH {ECO:0000313|EMBL:OFJ52492.1,
RC ECO:0000313|Proteomes:UP000178953};
RA Greninger A.L., Qin X., Jerome K., Vora S., Quinn K.;
RT "genome sequence of Mycobacterium sp. 739 SCH.";
RL Submitted (SEP-2016) 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:OFJ52492.1}.
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DR EMBL; MCHX01000039; OFJ52492.1; -; Genomic_DNA.
DR RefSeq; WP_070354364.1; NZ_MCHX01000039.1.
DR AlphaFoldDB; A0A1E8Q1S8; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000178953; 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; 5.
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:UP000178953}.
FT DOMAIN 1..74
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 882 AA; 92708 MW; 0891F25DC0202C31 CRC64;
MTVTVNGRPL PGEPRPGQCL RTYLRDHGHV EVKKGCDAGD CGACSVIVDG AAVHSCVYPA
FRAAGRAVTT VAGLGTPDDL HPLQRRFAEA AGFQCGFCTA GMITTAATLD SAVLEAATPD
AAEALAERLK GNLCRCTGYR AIGDALAGRR NVEKSEGAAD VGRSIAAPAG LRVVTGTEQY
TMDFAPSGLL HLAVLRSPVA HARIIAIDTA AAERLPGVRL VLTHRDGPRA AFSTARHDDR
RDDPDDTLVL DDVVRFVGQR VAAVVADDVA TAEAACRAIA VEYQELPAVL DPEAARLPDA
PKVHGDKGVE ARILDAGRNL VAAHHGEVGD VAAGIAAAER SGGAVVRGRW HTARVQHAHL
ETHGATGWRD EAGRLVVRTS SQVPFLVRDE LCHLFGLRPD DVHVFTRRVG GGFGAKQEML
AEDLVALAVL RLGLPVRYEF TRSEEFTGAP CRHPFRVDAT VAAGPDGVLT ALAVDVLVDA
GAYANHTVGV MFHGCGESVA VYRCPNKRVD AEAVYTNNIP SGAFRGYGLG QVAFAIESAL
DELALDLGID PFELRRRNVV VPGDPFVDTQ DGHHDLGFGS YGLDQCIDDA QRALHAGNGV
APPEGAHWRV GEGMALAMIA TIPPRGHHSE ASLTLGADGG YVLSVGTAEF GNGTSTVHAQ
LVAAEFDVPV ERVRIRQSDT DFTGYDTGAF GSAGTVVAGR AVRAACADLR ARLDAGGVAP
LTGHGRHDGT PRSVAFNVQA FRVAVDVRTG VVRILQSVQA ADAGVVLNPE QCRGQVEGGV
AQAIGSSLYE EMRVGPDGAV TTTELRNYHI PQLADVPVTE VHFADTVDEL GPLGAKSMSE
SPYNPVAPAL ANAIARACGA RLRRLPMTPA RVWRELHVSG AP
//
