ID H1PQY0_9FUSO Unreviewed; 587 AA.
AC H1PQY0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=HMPREF0402_00823 {ECO:0000313|EMBL:EHO82793.1};
OS Fusobacterium ulcerans 12-1B.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=457404 {ECO:0000313|EMBL:EHO82793.1, ECO:0000313|Proteomes:UP000003233};
RN [1] {ECO:0000313|EMBL:EHO82793.1, ECO:0000313|Proteomes:UP000003233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12_1B {ECO:0000313|EMBL:EHO82793.1,
RC ECO:0000313|Proteomes:UP000003233};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium ulcerans 12_1B.";
RL Submitted (JUL-2012) 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:EHO82793.1}.
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DR EMBL; AGWJ02000002; EHO82793.1; -; Genomic_DNA.
DR RefSeq; WP_008696228.1; NZ_KE161007.1.
DR AlphaFoldDB; H1PQY0; -.
DR PATRIC; fig|457404.5.peg.442; -.
DR HOGENOM; CLU_011398_4_0_0; -.
DR BioCyc; FSP457404-HMP:GTSQ-825-MONOMER; -.
DR Proteomes; UP000003233; 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 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.
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}; Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 22..587
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022271597"
FT DOMAIN 35..109
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 587 AA; 63419 MW; F53A79C4A0CF74CA CRC64;
MNKKRILALM LCAALSISAF GVEFKEGTYV GEAKGYRGEV KVEVKTSKNK IEEVKVIKNT
DTPIISESAA KKVPEQIVKY QSLRVDGVSG ATGTSRALTS AVRNALKNSG ADLKELNKKP
VIEAKKLVKE TQNKDVVVIG AGGAGLVAAI EAKNNGAKNV IVLEKMAFAG GNTLISGGEY
AAPNNWVQVK KGLKDSNDAF YNDILKGGDN EGDPKLVRVL ADNALSGAEW LKDYINMTFE
DRQMFFGGHS VERSLVPQGA TGVEMISKLL AKAEELNIPV LYETPATELI VDKGRVTGVK
AVSEDKEYTF LAKDGVILAT GGFGSNLEMR VKYNKDVDEN ILSTNTVGIT GDGITMAEKI
GAQLEDMPFI QTYPTCDPIS GALLYFGDVR LVGGSILVNQ EGKRFVEELE RRDVISMAIK
NQTGNAAYQF CDEAQVKLSG VAEHHADEVN YLFNNKLLVK ADTIKEAADF FGIDATELEK
TVAKYNQYAK DGKDLEFNKR GKLTPFEAKG PFYIMKAVPA VHHTMGGIKI DENARVINTK
GEVIKGLYGA GEVTGDIHGT NRLGSDAIAD ITVFGRIAGQ NVVKDNK
//
