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
//