ID R7AH32_9CLOT Unreviewed; 973 AA.
AC R7AH32;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aldehyde oxidoreductase Mop3 {ECO:0000313|EMBL:CDD54844.1};
GN ORFNames=BN653_00709 {ECO:0000313|EMBL:CDD54844.1};
OS Clostridium sp. CAG:43.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262805 {ECO:0000313|EMBL:CDD54844.1, ECO:0000313|Proteomes:UP000018284};
RN [1] {ECO:0000313|EMBL:CDD54844.1, ECO:0000313|Proteomes:UP000018284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:43 {ECO:0000313|Proteomes:UP000018284};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD54844.1}.
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DR EMBL; CBHG010000058; CDD54844.1; -; Genomic_DNA.
DR AlphaFoldDB; R7AH32; -.
DR STRING; 1262805.BN653_00709; -.
DR Proteomes; UP000018284; 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:UP000018284}.
FT DOMAIN 4..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 973 AA; 106438 MW; D289F75697CFBB55 CRC64;
MKLRKMMLNI NGVDRMFMCD PENDKLSDVL RRIGLTGVKV GCGTGVCGSC SIILNGQVIR
SCTKKISQVE EYSKITTIEG IGTPQHLHPL QVAWMNCGAV QCGFCVPGFI VSAYALLEQN
PDPTREEVRD WFQKTRNVCR CTGYKQIVDA VMAAAKVMRG ECSIEDIKFH NPEDGNYYGK
PVVRQDALGK VCGLTDYGDD QALKMPQGVL YAAIVQPKVT HHAKILAIHT EEAEKMPGVV
KVITAKDLIA AGGTNIMAEG QFHERSTVMT PSRKVLQDEK IYRYGDVIAM VVAHTHRQAR
AAAAKVTMEY EQLPEYLTYL DAVMPDAIRI HEDTPNIFCE QPVLKGAGLE DAEEVRDLID
KAPHVVEGSF SSSREPHLSI EGCVLQSYWG DDGLLTIQCK SQCVYSSIGR LGNCLGVPKD
KYRIIMNPTG ASFGWSTNAG DIALCAACTV VTGEPVSLSM SYEEHQHFSG KRCPAYSNGR
LACDNEGKIL AAEFDIGMDH GAYSWGGDDV MTKPARFTFF PYNVPNVAGL VRVANVNHAF
GTAYRSYGSP QAYTLSEPLM DMMAEELGMD PFEFRYKNIC REGDKNINSY VYPQYPMEKI
MDTMRPIYEK AVADAKAADT PEKRRGVGIA WGGFNVTEGG GDSAEVALEL MPGNKIRKYD
TWHAMGQGAT TGSLVVTLEA LKEMHLTPED IQLIQNDTKT CPDTGMAGAS RSLYMDGNAT
IIAANKLLAA MRKEDGTLRT YDEMKAEGIE TKYLGRYETN TTPGLCRLDP NTGIGDPTPA
FTYCLNLAEV EVDTKTGKTT VLKFTCVDFV GRIGNIDAVN GQAYSGIMHG IGFALKEDYA
DVKKHANMFG AGTSYIKDVP DDINLIHIDG AISDGPFGSS GASEAFQASG HCAVLNGIYN
ACGVRIHEIP ALPEKVKAGL DAIAKGEKPY EPKKYFLGSD MYEELENIKE NPVQVGTQSF
YVSLDDPTAE RPF
//
