ID Q895T9_CLOTE Unreviewed; 571 AA.
AC Q895T9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AAO35751.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:AAO35751.1};
GN OrderedLocusNames=CTC_01178 {ECO:0000313|EMBL:AAO35751.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO35751.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO35751.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AE015927; AAO35751.1; -; Genomic_DNA.
DR AlphaFoldDB; Q895T9; -.
DR STRING; 212717.CTC_01178; -.
DR KEGG; ctc:CTC_01178; -.
DR HOGENOM; CLU_003291_1_2_9; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AAO35751.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 469..553
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 571 AA; 63047 MW; 1E3534664D180C51 CRC64;
MEGYAMSKKY LIVGGVAGGA STAARLRRLS EEDEIIMFER GPHVSFSNCC LPYHLAGLIK
TANQLVLMSP EQFKKQYNIE ARVNSEVIDI DRAKKEITIK DTLTGKEYTE NYDKLILSPG
AKPIVPPIKG IEDINLFTVR NVIDIDKLNK FVSTMKTKNA TVVGGGFIGI EVAENLKEAG
FNVTLVEAMP QVMKIFDYDM VQILHKELHD KGINLIVNDK VASFEKDTVV LESGKRVEAE
AVVMAIGVTP ETDLAVKAGL ELGELGGIKV DQNYRTKDED VYAVGDAIEV YHALTGKMTK
LPLAGPAQKQ AREVADHIHG RLVPNTGYIG SSVVKCFEYN GASTGLNEGM IKALNLDIQY
ETVKVIPGDK VGLMPGCEPL HFKLLFEIPT GKILGAQAIG RGNVDKRVDV IATAIKFGAT
INDLRDLEFC YAPPFGTAKD VVNFAGYVGS NLLHDEFKQV HEYDVRDLVE SGACIIDVRE
KHEYELSHII GAKNIPLSEI RDRVAEIPKD QPVYLHCRSA QRSYNAAKAL KHLGFDNIYN
VSGGFMGISF YEYFNDQTTG REKIVTDYNF L
//
