ID D0BM77_9LACT Unreviewed; 585 AA.
AC D0BM77;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=HMPREF0446_01080 {ECO:0000313|EMBL:EEW93092.1};
OS Granulicatella elegans ATCC 700633.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Granulicatella.
OX NCBI_TaxID=626369 {ECO:0000313|EMBL:EEW93092.1, ECO:0000313|Proteomes:UP000002939};
RN [1] {ECO:0000313|EMBL:EEW93092.1, ECO:0000313|Proteomes:UP000002939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93092.1,
RC ECO:0000313|Proteomes:UP000002939};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEW93092.1, ECO:0000313|Proteomes:UP000002939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93092.1,
RC ECO:0000313|Proteomes:UP000002939};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Granulicatella elegans ATCC 700633.";
RL Submitted (OCT-2011) 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:EEW93092.1}.
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DR EMBL; ACRF02000016; EEW93092.1; -; Genomic_DNA.
DR RefSeq; WP_006703356.1; NZ_KI391971.1.
DR AlphaFoldDB; D0BM77; -.
DR STRING; 626369.HMPREF0446_01080; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_0_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000002939; 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 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:UP000002939};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 28..585
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022249847"
FT DOMAIN 37..111
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 585 AA; 63423 MW; A9E55E8F908A1220 CRC64;
MKNSKFNFIF MLLSMILVLV GCSPSKNSGS FEGIGTGKHG EIKVMVSIKD AKITKIDITK
QSENKVLADK VYKELSTNII SKNSADIDVV SGATATSEGY LEAVKDALKK SGINLASVTN
KIKDSEQIPT EQTFDVVVVG SGGAGFSAAI EAKEAGKSVA IIEKLPAVGG NTLISGGEMN
APENWVQKNL GITGDSVESY YEDTIKGGDH AANPSLVKIM AEKALESAEW LKDEIHVEFL
SDQLFRFGGH SYKRALIPVG HTGAELISKL NAKADELKIP IFLNVKAEKL INNSNGRVIG
VKANDKNKKE LTFNANNAVV LTTGGFGSNV EMRTKFNKEY DSRYKSTDSV GTTGDGIIMA
QEVGAALNNM EYIQTYPIAN PKTGMISLLA DTRFDGAILI NQEGKRFVEE LDRRDVISKA
ILAQTGGYTY QLWNDDIDAI SKTKEAHKAE YDELIREKLL VKADTLEEAA TFFNIDINNL
KDTISKVNMY AKEKDDKDFH HRGGLVSLEN GPYYIQKAVP SVHHTMGGLV INEKTEVLNE
NGEPIPGLYA AGELTGVIQG KNRLGGNAIT DIITFGRIAG KQVAN
//
