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Database: UniProt
Entry: K4LQP5_THEPS
LinkDB: K4LQP5_THEPS
Original site: K4LQP5_THEPS 
ID   K4LQP5_THEPS            Unreviewed;       525 AA.
AC   K4LQP5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Molybdopterin containing oxidoreductase YoaE {ECO:0000313|EMBL:AFV10419.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:AFV10419.1};
GN   Name=yoaE {ECO:0000313|EMBL:AFV10419.1};
GN   OrderedLocusNames=Tph_c01710 {ECO:0000313|EMBL:AFV10419.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV10419.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV10419.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA   Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of the
RT   fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(2012).
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP003732; AFV10419.1; -; Genomic_DNA.
DR   RefSeq; WP_015049339.1; NZ_KI912609.1.
DR   AlphaFoldDB; K4LQP5; -.
DR   STRING; 1089553.Tph_c01710; -.
DR   KEGG; tpz:Tph_c01710; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   Proteomes; UP000000467; Chromosome.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:AFV10419.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000467}.
FT   DOMAIN          4..291
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          400..489
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   525 AA;  59266 MW;  D350915D1ACBC1F9 CRC64;
     MKRGTKLIVV DPRANWLATR AEHHLQLRPG TDGALALALL YAVIKTDKYD KQFVEKWCYG
     FDKLAERVAQ YPPEWAEEIT GVPAEDIYAA AECLVQKPSS ACTGVAIDQN PNCIQIAHAL
     YSIFAITGNL DIPGGLFMGQ PQFFAGAAVD SNEDEEEFEG IGYREFPAIP MIVNTTHPDC
     TLEALETGKP YPIKFAFIQS TNFLASSIVV QPKRWYEAMR KLEFIVASDI FMNPTIMALA
     DLVLPVSTSL EHDGIVMNSM ASQPGQFGAL VKIIDDFGET KSDLEIVLDL YHRLYPDSND
     PRWKDPESYL THDMVQIPGI GVTFPELKER VIGQYELEYR KYEKGLLRAD GKPGFNTPTG
     KIELYSTILA SLNEDPLPYY IEPKFSAVSR PDIAKEYPLI MTTGARRFTY FHSEHRQISK
     LREIHPWPTA EINPKTAAEK GITEGSWIYI ENPWGKAKVV AHVTPIVKEN VVSVDHGWWY
     PERDPEKLFD VWEPSINSLI PHKEIGKLGF GTHYKCMPCK IYRAE
//
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