ID A0A1W1ZDA7_9FIRM Unreviewed; 972 AA.
AC A0A1W1ZDA7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aldehyde oxidoreductase {ECO:0000313|EMBL:SMC46141.1};
GN ORFNames=SAMN04488500_103182 {ECO:0000313|EMBL:SMC46141.1};
OS Sporomusa malonica.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=112901 {ECO:0000313|EMBL:SMC46141.1, ECO:0000313|Proteomes:UP000192738};
RN [1] {ECO:0000313|EMBL:SMC46141.1, ECO:0000313|Proteomes:UP000192738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5090 {ECO:0000313|EMBL:SMC46141.1,
RC ECO:0000313|Proteomes:UP000192738};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; FWXI01000003; SMC46141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1ZDA7; -.
DR STRING; 112901.SAMN04488500_103182; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000192738; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192738}.
FT DOMAIN 4..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 972 AA; 106251 MW; EF2F086C24F8DE33 CRC64;
MKLRKMWFNI NGADRMVVCC PEKDTLSDVL RRIGLTSVKV GCGTGVCGSC AVILDKKVVR
SCNKKIKAVE EYSKIITLEG IGTPSNLHPL QVAWMNCGAV QCGFCTPGFI VSAYALLLEN
NNPTREEVRD WFQKTRNVCR CTGYKQLVDA VMAAAKVVRG EAKIEDITFQ LPEDNECYGK
PVVRPTALSK VTGLADYGED MAVKMPGETL HVAVAQPRIA HHANILKIDT SEAEKMPGVV
KVITYKDILA NGGTNQMAEA NLHERSTVTL PSRKILCDER IFRYGDVVAL AIANTPDQAR
AAAAKVKVEI EQLPEYLNYL DAVLPDSIRV HDDTPNIFCL QPVLKGVALE NADNVIKVLD
ESAHSVEGSF YSAREPHLSI EGCTVQAYFD EEDCLTFQCK SQGQYTSISR IGNSLGIPRK
KLRIVNNFNG ASFGWSTNAG DLVLAGAAAV AVNGPVALHM SYEEHQHYSG KRCPSYSNGR
AACDENGKIT AVEFDIGLDH GAYSWGGDHV IEKPVRFTFF PYHVPHVAGL GRVANTNHTF
GTAYRSYGSP QAYTLSEALV DMLAEKAGID PFDFRWLNIA RLGETNINSF PFKDYPMEDM
MNKMRPFYEK AVAEAKAADT PEKRRGVGLA WGGFNVTEGG TDQATIILEL APDNMILKYD
TWQDLGQGGD IGSLMVTLEA LKPMGVTSDR IRLIQNDTKV CPDSGMSAAS RSHYMNGHAT
KIAAERLMNA MRKPDGTYRT YEEMVAEGIE TKYEAQYLCT ATPVIRIDPN TGVGDPTPAY
TYVLNLAEVE VDTATGKTRV IRFVCIYDVG KIGNIDAVSG QAYGGISHSI GFALSEDYSD
VKKHTNIAAS GVPYIKDIPD EIILIPCDNP RSDGPFGSSG ASEAFQSSGH VAVLNAIYNA
CGVRIYEMPA RPEKVKAGLE ILAKGGKIEP PQKYFLGSDL YEELENIKAN PVVFRGDDMF
TALGGSTDER FY
//
