ID   A0A3Q9I9L9_9BACL        Unreviewed;       598 AA.
AC   A0A3Q9I9L9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=EI981_16270 {ECO:0000313|EMBL:AZS15838.1};
OS   Paenibacillus lutimineralis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS15838.1, ECO:0000313|Proteomes:UP000270678};
RN   [1] {ECO:0000313|Proteomes:UP000270678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA   Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT   "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL   Submitted (DEC-2018) 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; CP034346; AZS15838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9I9L9; -.
DR   KEGG; plut:EI981_16270; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000270678; Chromosome.
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   PRINTS; PR00368; FADPNR.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000270678};
KW   Signal {ECO:0000256|RuleBase:RU366062}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT   CHAIN           25..598
FT                   /note="Urocanate reductase"
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT                   /id="PRO_5039750001"
FT   DOMAIN          51..125
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   598 AA;  63605 MW;  F590F3A64C556F2D CRC64;
     MMKMKRIGSL ILILSLVVML AACGSGNNKG KEADNGAGQN GIVTSIGEGD GKHGTIKVEV
     TFENNEIKNI KVLEQKENEV LAEPVFKELG DTIIASNSAE VDAISGSTVT STGYIDAVKD
     AIAKSGLTLV AKQAAGKSET DEPAEQTYDV VIIGAGGAGF SAALEAKQAG ASVVLLEKMP
     SVGGNTLISG GEMNAANTWV QEKLGIKDSV DLFAEDTLKG GDNVGDPEMV RVLAENATAA
     AEWLKNDIKV NFLEDNLFQF GGHSVKRALI PEGHTGAELI TKLKTKLDEM KIDLKTNTKA
     DKLLTDDSGK VVGVEATGAN GNKITFHANK GVVIASGGFG SNVEMRKQYN PEFDEKYMTT
     DAPGSTGDGI VMAQDIGAAL TNMESIQTYP VCDPVTGVIS LVADSRFDGA ILVNQSGKRF
     VEELERRDVI SRAILAQEGG YAYQLWNQEI GDISKTVDVH KDEYDALVKE GVLYKADTLK
     EAAEFFKIDP KALQETIDRV NKFAKAGNDE DFHHRQGLHD MSKGPYYIEK AVPSVHHTMG
     GLVINKTTQV MNEKGEPIPG LFAAGEVTGV IHGTNRLGGN AIADAITFGR IAGQEVAK
//