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Database: UniProt
Entry: H1PTN8_9FUSO
LinkDB: H1PTN8_9FUSO
Original site: H1PTN8_9FUSO 
ID   H1PTN8_9FUSO            Unreviewed;       569 AA.
AC   H1PTN8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=HMPREF0402_01781 {ECO:0000313|EMBL:EHO80708.1};
OS   Fusobacterium ulcerans 12-1B.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=457404 {ECO:0000313|EMBL:EHO80708.1, ECO:0000313|Proteomes:UP000003233};
RN   [1] {ECO:0000313|EMBL:EHO80708.1, ECO:0000313|Proteomes:UP000003233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12_1B {ECO:0000313|EMBL:EHO80708.1,
RC   ECO:0000313|Proteomes:UP000003233};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium ulcerans 12_1B.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + dihydrourocanate = AH2 + urocanate; Xref=Rhea:RHEA:36059,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:27247,
CC         ChEBI:CHEBI:72991; EC=1.3.99.33;
CC         Evidence={ECO:0000256|RuleBase:RU366062};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU366062};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU366062};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|RuleBase:RU366062};
CC       Note=Binds 1 FMN covalently per subunit.
CC       {ECO:0000256|RuleBase:RU366062};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|RuleBase:RU366062}.
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:EHO80708.1}.
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DR   EMBL; AGWJ02000021; EHO80708.1; -; Genomic_DNA.
DR   RefSeq; WP_008697321.1; NZ_KE161008.1.
DR   AlphaFoldDB; H1PTN8; -.
DR   PATRIC; fig|457404.5.peg.2321; -.
DR   HOGENOM; CLU_011398_4_0_0; -.
DR   BioCyc; FSP457404-HMP:GTSQ-1791-MONOMER; -.
DR   Proteomes; UP000003233; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1010.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF04205; FMN_bind; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00900; FMN_bind; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366062};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU366062};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366062}; Signal {ECO:0000256|RuleBase:RU366062}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT   CHAIN           23..569
FT                   /note="Urocanate reductase"
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT                   /id="PRO_5022261665"
FT   DOMAIN          31..104
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   569 AA;  59707 MW;  DD5E6ADDCED71AFB CRC64;
     MRKKLLCLLS ALTIMISSVA SAKTIEGVGA GYKGDIKVNV TYEGNEIKGV EILKHEETAF
     TKKAMEQVTK EIVENQSVEV DNVAGATYTS EGIKEAVGAA VAQAGIKLVS KAPAKKADAV
     LTDISTDIVV VGGGGAGLTA AIAAKEKGAN VILLEKMAML GGNTNYATGG INAANTSLQK
     KLGIEDSEEL FYNDTMKGGK NKNNPELLKK MTDESKHIID WLISKGTDLT EVSFSGGQSV
     KRIHRPTGGK AVGPVVVAAL SDTADKLGIE IRTESEVTKL IKTGDKVTGV EVKHKGQTYV
     ISAKAVVMAT GGFGANPAMI EEYNPALKGF GSTNSPAITG EGIKMVKAAG ADLVDMPEIQ
     THPTVVHNNT AMITESVRGE GAILINRDGK RFINELETRD VVSKAELAQK GASAFLVFDQ
     GTRENLSAIN GYVKQGFAVE ASTLEELAGK VGIEPKTFVE TITTYNGYVK AGEDKDFGKK
     GLPRELVKAP FYAIEVSPAI HHTMGGVRIN TDTQVLTPEG KVIPGLYAAG EITGGVHGGN
     RIGGNAVTDI TVFGKIAGEN AADFVKNSK
//
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