ID A0A1F2PEX2_9FIRM Unreviewed; 908 AA.
AC A0A1F2PEX2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aldehyde oxidoreductase {ECO:0000313|EMBL:OFV69422.1};
DE EC=1.2.99.7 {ECO:0000313|EMBL:OFV69422.1};
GN Name=mop {ECO:0000313|EMBL:OFV69422.1};
GN ORFNames=ACWI_30700 {ECO:0000313|EMBL:OFV69422.1};
OS Acetobacterium wieringae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV69422.1, ECO:0000313|Proteomes:UP000176244};
RN [1] {ECO:0000313|EMBL:OFV69422.1, ECO:0000313|Proteomes:UP000176244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV69422.1,
RC ECO:0000313|Proteomes:UP000176244};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Acetobacterium wieringae DSM 1911.";
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:OFV69422.1}.
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DR EMBL; LKEU01000040; OFV69422.1; -; Genomic_DNA.
DR RefSeq; WP_070372329.1; NZ_LKEU01000040.1.
DR AlphaFoldDB; A0A1F2PEX2; -.
DR STRING; 52694.ACWI_30700; -.
DR OrthoDB; 9759099at2; -.
DR Proteomes; UP000176244; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0033727; F:aldehyde dehydrogenase (FAD-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 ECO:0000313|EMBL:OFV69422.1}.
FT DOMAIN 2..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 908 AA; 98266 MW; CC3A608A034F8794 CRC64;
MEKKTLFING IQRTVIVDPE TTLANLIRKQ QGLTGTKVGC GKAECGACSV ILNGKVVRSC
VTKMKKVDDE SEIITIEGVG AHDNLHPLQL AWMVNGAAQC GFCTPGFIVS AKALLEENAS
PTREEVRAWF QKHRNVCRCT GYIPIVDAVM DAAKLMRGEI TKEDLWFQLK EGASIMGSTM
ARPSALAKVT GTWDFGADLG LKLPENTLHI KLVQAQVSHA NIISVDTSEA EKMEGVFKVI
TAKDVPGTNR INGLAFPQNL GDGLERPILN DKKIFQFGDA IAMVLADTPE QAEAAAAKVV
VEIEELLPYM SAPAAMAEDA IEIHPGTPNI YFTTNVVKGD ETAPLMEKLP NVIEDDFYIG
RQPHLPLEPD VGFAYFDEED NLMVHSKSIA LHFHQLMTAE AIGVDPTKYF IVQNPTGGTF
GYKFSPTIEG LLGVAALVTK RPVYLEFNMY QQITYTGKRS PFFMNVKMGA DENGILKAME
TDWSVDHGPY CEFGDLVTTR GSQFIGAGYN IPNIRGEGRT VATNHAWGSA FRGYGSPQSL
FASETLIDML AYQMGEDPLE LRYKNVYREG DTTPNGCEPD VIALPQAIDT IRPIYQAAKA
KAEALNAEGG DIKHGVGISL NIYGCGLDGP DSSEMWIELT KDGVIVGDSW EDHGQGADMG
TLTFAHETLR PLGIKPEQIK LVMNNMKLTP NSGPAGGSRS NVMTGNAIKV GCENLLAAMK
KADGTYRTYD EMVAEGLPLR YEGVWTAPCT APSVETSQGN PFPVYMYGVL LSEVSVDTTT
GKTHVDKLTL VSDCGTITNK TVLEGQLWGG LTQGIGLALS EDFEDLKKHT TLTGCGIPQV
KDVPDEIVLI HQETPRPLGP YGAAGSGEMP LSAPHASIAN AIFNACGVRI KHLPAYPEKV
LEGLEALK
//
