ID A0A2M8GYQ8_9VIBR Unreviewed; 806 AA.
AC A0A2M8GYQ8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=CSW98_09605 {ECO:0000313|EMBL:PJC86457.1};
OS Vibrio sp. HA2012.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1971595 {ECO:0000313|EMBL:PJC86457.1, ECO:0000313|Proteomes:UP000232179};
RN [1] {ECO:0000313|EMBL:PJC86457.1, ECO:0000313|Proteomes:UP000232179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA2012 {ECO:0000313|EMBL:PJC86457.1,
RC ECO:0000313|Proteomes:UP000232179};
RA Wang K.;
RT "The draft genome sequence of Vibrio sediminis HA2012.";
RL Submitted (NOV-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}.
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:PJC86457.1}.
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DR EMBL; PFXK01000004; PJC86457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8GYQ8; -.
DR OrthoDB; 8523426at2; -.
DR Proteomes; UP000232179; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000232179}.
FT DOMAIN 200..274
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 806 AA; 87473 MW; E551F313E617E92E CRC64;
MKFTAIVGTS SPKSYNRTLL QFMQAHFKDK AEIQLLEINE VPMFNQDTPS NNPQLLKINE
NIIASDGVII ATPEYNHSIP SSLKSVLEWL SYELHPLDGK PVMILGASID SQGSSRAQLH
LRQILDAPGV NANVMPGYEF LLGNAHKAFD ENGQLSSEGT IDFLEICFLR FMRFAKISNQ
LNQEEDFSFA PGTYDVHALG HGGALPMKVS FSEKKIESIN IDTAGETEGL ADVVFVRIPD
KIIEGQTLNV DALSGASETS NAVIDGVAKA VKLAGVNPDI LKKRPKPASS LNRGDEEYTC
DVVVIGGGGA GLSAAATVLQ EGKSAIVLEK YPAVGGNTIR TGGPVNAADP EWQKTFQENP
GERHTIEALL STPESDIHAE YLPDFRALKE EFAAYQQQFG DEKGYLFDSP LLHRMQTYFG
GKRTDLQGNN IYGQYDLVKI LTDHALESVQ WLEDIGVEYD KSIVFAPVGA LWRRGHKPVK
KYGTAFILAL SKYIEEMSGT IITDSPAKEF LIEKGEIKGV IATGVNGQKI TVRAKAVVLA
SGGFGANTKM LQQYNTYWSN IADDIKTTNS YAMTGDGILL GQSVGAGLTG MGFTQMMPVA
DPNTGELFSG LQVPPENFVI VNKQGKRFIN EFAGRDVLTK AALAEGGLFY LIADDEIKKT
AANTSQEKID RQVEAGTLFR ADTLEELAIK VGMDPAVLVD TVNKYNSYVE AAEDPEFHKD
TFSLKVEKAP FYATPRQPAV HHTMGGLKID TATRVLDENN QPIKNLYAAG EVAGGIHAGN
RLGGNALADI FTFGRIAGKT AIEAMS
//
