ID   A0A1N6P674_9GAMM        Unreviewed;       806 AA.
AC   A0A1N6P674;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=SAMN05880558_101458 {ECO:0000313|EMBL:SIP99898.1};
OS   Aeromonas sp. RU39B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIP99898.1, ECO:0000313|Proteomes:UP000186911};
RN   [1] {ECO:0000313|EMBL:SIP99898.1, ECO:0000313|Proteomes:UP000186911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU39B {ECO:0000313|EMBL:SIP99898.1,
RC   ECO:0000313|Proteomes:UP000186911};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTMJ01000001; SIP99898.1; -; Genomic_DNA.
DR   RefSeq; WP_076573862.1; NZ_FTMJ01000001.1.
DR   AlphaFoldDB; A0A1N6P674; -.
DR   STRING; 1907416.SAMN05880558_101458; -.
DR   InParanoid; A0A1N6P674; -.
DR   OrthoDB; 8523426at2; -.
DR   Proteomes; UP000186911; 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; 3.40.50.360; -; 1.
DR   Gene3D; 3.90.1010.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR005025; FMN_Rdtase-like.
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; 2.
DR   Pfam; PF04205; FMN_bind; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   SMART; SM00900; FMN_bind; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 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}.
FT   DOMAIN          200..274
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   806 AA;  87655 MW;  2BB22E5EE6E363B2 CRC64;
     MKFTALVGTT SPSSYNRTLL QFMQTHFNDK ASIELLEIVG IPMFNQDLPS NHPLLLAIHN
     KIVESDGVII ATPEYNHSIP SSLKSLLEWL SYELHPFDGK PVMILGASID AQGSSRAQLH
     LRQILDAPGV NANVMPGYEF LLGNAHKAFD ENGRLSSEGT IDFLERCFLR FMRFAKISNQ
     LNEEEDFSFT PGTYEVHALG HGGALPMKVA FSEKKIESIN IDTAGETEGL ADVVFVRIPD
     KIIEGQTLNV DALSGASETS HAVLDGVAKA VKLAGVNPDI LRRRPKPASS LNHGDEEYTC
     DVVVIGGGGA GLSAAATVLQ QGKRAIILEK YPAVGGNTIR TGGPINAADP DWQRTFQENP
     GERHTIEALL GTPESEIHPE YLGDFRALKD EFSSYQALFG HNKGYLFDSP LLHRMQTYFG
     GKRTDLQGNS IYGQYDLVKI LTDQALESVK WLEEIGVEYD KSIVFAPVGA LWRRGHKPVK
     KYGTAFIVAL KEYIERMSGT ILTDSPAKEF LLENGEIKGV VATGVNGQKI TVRAKAVVLA
     SGGFGANTKM LKQYNTYWNY IADDIKTTNS YAMTGDGILL GQSVGAGLTG MGFTQMMPVA
     DPITGELFSG LQVPPENFVM VNKQGKRFVN EFAGRDVLTK AALAEGGLFY LIADDEIKKT
     AANTSQEKID RQVEAGTVFR ADTLEELAVK VGIAPDVLVN TISRYNSYVE AGEDPEFHKD
     TFSLKVEKAP FYATPRQPAV HHTMGGLKID TFARVLDENN QPIKNLYAAG EVAGGIHAGN
     RLGGNALADI FTFGRIAGKT AVEAIS
//