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Database: UniProt
Entry: A0A0W8JB91_9VIBR
LinkDB: A0A0W8JB91_9VIBR
Original site: A0A0W8JB91_9VIBR 
ID   A0A0W8JB91_9VIBR        Unreviewed;       806 AA.
AC   A0A0W8JB91;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=VRK_34630 {ECO:0000313|EMBL:KUI97492.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI97492.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI97492.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI97492.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-2015) 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:KUI97492.1}.
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DR   EMBL; LQIY01000026; KUI97492.1; -; Genomic_DNA.
DR   RefSeq; WP_059122348.1; NZ_KQ947475.1.
DR   AlphaFoldDB; A0A0W8JB91; -.
DR   STRING; 1761910.VRK_34630; -.
DR   PATRIC; fig|1761910.3.peg.3503; -.
DR   OrthoDB; 8523426at2; -.
DR   Proteomes; UP000054473; 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;  87889 MW;  AB39AD31478B4C11 CRC64;
     MKFTAIVGTT SPKSYNRTLL QFMQAHFKDK ADIELLEIDQ VPMFNQDQPS TNPQLLEINQ
     KIIASDGVII ATPEYNHSIP SSLKSVLEWL SYELHPLDGK PVMILGASID AQGSSRAQLH
     LRQILDAPGV NANVMPGYEF LLGNAHQAFD DQGQLNNEGT IDFLEICFFR FMRFAKISNQ
     LNVEEDFSFA PGTYEVHALG HGGALPMQVS FSEKKIESIH IDTAGETEGL ADVVFVRIPD
     KIIEGQTLNV DALSGASETS HAVIDGVAKA VKLAGVNPDI LKKRPKPASS LNRDDQEYSC
     DVVVIGGGGA GLSAAATVLQ AGKNAIVLEK FPAVGGNTIR TGGPINAADP EWQRTFDENP
     GERHTIEALL STDESEIHPE YLADFRALKE EFAAYQQQFG DQKGYLFDSP LLHRMQTYFG
     GKRTDLEGNS IYGQYDLVKI LTDHALESVQ WLEEIGVEYD KDVVFAPVGA LWRRGHKPVK
     RYGTAFILAL SRYIESMSGT ILTDSPAKEF LIEDGEIKGV IATGVNGQKI TIHAKAVVLA
     SGGFGANTKM LQQYNTYWSH IADDIKTTNS YAMTGDGIVL GQSVGAGLTG MGFTQMMPVA
     DPNTGELFSG LQVPPENFVI VNKQGKRFIN EFAGRDVLTK AALAEGGLFY LIADDEIKKT
     AANTSQEKID RQVEAGTLFR ADTLEELAVQ VGMEPDVLVE TISKYNRYVE AGHDPEFHKD
     TFSLKVEKAP FYATPRQPAV HHTMGGLKID TATRVLDENN RPIKHLYAAG EVAGGIHAGN
     RLGGNALADI FTFGRIAGKT AMSEMD
//
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