ID D2MNN8_9FIRM Unreviewed; 615 AA.
AC D2MNN8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=HMPREF9013_0021 {ECO:0000313|EMBL:EFC05829.1};
OS Bulleidia extructa W1219.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Bulleidia.
OX NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC05829.1, ECO:0000313|Proteomes:UP000005017};
RN [1] {ECO:0000313|Proteomes:UP000005017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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:EFC05829.1}.
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DR EMBL; ADFR01000004; EFC05829.1; -; Genomic_DNA.
DR RefSeq; WP_006627009.1; NZ_ADFR01000004.1.
DR AlphaFoldDB; D2MNN8; -.
DR STRING; 679192.HMPREF9013_0021; -.
DR eggNOG; COG1053; Bacteria.
DR eggNOG; COG3976; Bacteria.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000005017; 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; 2.
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.
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:UP000005017};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 21..615
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5039752726"
FT DOMAIN 38..112
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 615 AA; 64899 MW; 5E27DCD6C756FCE7 CRC64;
MKKFLSVVLL AFTLILSGCA PKSGFSFKAG TYTGTAKGRN GDVTVEVTLS EKKIEKVVVT
KQDETKAIAQ AALEKIPNAI VKNQSLAIDA VSGATLTSKA ILAASEEAIK SSGADVSALK
KVSKKAVKKE ETLDTDVVIV GAGGAGLTAA IAAKKAGKNV IVLEKRAISG GNSMLSTGGM
NAAKTKLQDK NKFKEGAGVE KTLKKAEKYP ELKSLANQVK AEYAEYQKKP NGYFDSIHLF
VLDTLVGGQN KNNRTLVETL AKNSASAIDW LKENGADLSQ VGSFGGASVK RIHKPVNKEG
KTIAVGSYLV PILQKKAEEL GVKIIYEAPV KEILMKDGAA VGVKADGYKV NAKSVVLTTG
GFAGNSEMVE KLKPELKGMA TTNTSGIVGD GIKMAEAIGA NTVDMNQIQI HPTVEYESKS
LITEGLRGDG AILVNSEGKR FFDEVGTRDA VSQAELKQKG GFAWLIVDQR MVDKSSVIAG
YIKKGYTKTG KTAEELAKAI GADEANLVNT LKTWNKYVAN RKDPEFNRTS FAKPLDKAPY
YAIKVSPGVH HTMGGIQINE KAEVLNKEGK VIANLFAAGE VTGGVHGANR LGGNAVADFV
VYGRIAGTNA AGNAK
//
