ID   A0A1G8Y7E2_9CLOT        Unreviewed;       593 AA.
AC   A0A1G8Y7E2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=SAMN05660472_00453 {ECO:0000313|EMBL:SDJ98726.1};
OS   Natronincola ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Natronincola.
OX   NCBI_TaxID=393762 {ECO:0000313|EMBL:SDJ98726.1, ECO:0000313|Proteomes:UP000198718};
RN   [1] {ECO:0000313|EMBL:SDJ98726.1, ECO:0000313|Proteomes:UP000198718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18346 {ECO:0000313|EMBL:SDJ98726.1,
RC   ECO:0000313|Proteomes:UP000198718};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNFP01000001; SDJ98726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8Y7E2; -.
DR   STRING; 393762.SAMN05660472_00453; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000198718; 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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198718};
KW   Signal {ECO:0000256|RuleBase:RU366062}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT   CHAIN           23..593
FT                   /note="Urocanate reductase"
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT                   /id="PRO_5039743486"
FT   DOMAIN          44..118
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   593 AA;  64361 MW;  C0E3ADC01CE1D479 CRC64;
     MLKTKKILSL LLALILITTA LVGCGNDAKE TLYQDGIYQG SAQGHNAEVE VEVTVKDGKI
     AEIEVLQHHE TKVLTDPVFE KAIPAIISEN SVNIDTFTGA TITSLALKNA IKDALTKAGG
     NEDVFKKGKL LKFDSASDSS EETYDVVVIG AGGAGLIAAI EAKAHGANVV ILEKMPFVGG
     NTLVSGGEFN APNTWVQEKL GIEDSVEQYY TDTLKAGDFE GDEELIRTLA ENITEGGEWL
     RDSVNVEFIE DYLMHFGGHS VPRAIYPIGG SGVELIQKLG AHAEAKDIPI KLSMKAEKIL
     TDDNDRVVGV EATDVTGRTV TFHAEKAVII ATGGFGANYE LTKKYNSEID ERYKGTIQKG
     TMGDGILMAE EIGADLMGME HIQTYPTCNP LTGNLSYVAD TRFDGAVLVN KEGQRFVEEM
     ERRDVISKGI LAQTDSIAYL VWDKTIKENS HMDKYQVEFD NMEKQNLIIK ADTLEEAAAF
     FDIDEKQLLE TIKTYNGYVQ EGQDKDFNRR GKLVALTEGP YYIQKVAPAI HHTMGGIKIN
     SEARVIDKDG NPIEGLFAAG EVTGGIHGTN RLGGNAISDL IVFGRIAGQT AAK
//