ID F3QGT1_9BURK Unreviewed; 721 AA.
AC F3QGT1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=HMPREF9439_00120 {ECO:0000313|EMBL:EGG57791.1};
OS Parasutterella excrementihominis YIT 11859.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=762966 {ECO:0000313|EMBL:EGG57791.1, ECO:0000313|Proteomes:UP000005156};
RN [1] {ECO:0000313|EMBL:EGG57791.1, ECO:0000313|Proteomes:UP000005156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11859 {ECO:0000313|EMBL:EGG57791.1,
RC ECO:0000313|Proteomes:UP000005156};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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:EGG57791.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFBP01000003; EGG57791.1; -; Genomic_DNA.
DR RefSeq; WP_008863314.1; NZ_GL883676.1.
DR AlphaFoldDB; F3QGT1; -.
DR GeneID; 43347671; -.
DR eggNOG; COG1053; Bacteria.
DR eggNOG; COG3976; Bacteria.
DR HOGENOM; CLU_011398_4_0_4; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000005156; 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; -; 2.
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; 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; 2.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00900; FMN_bind; 2.
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..721
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022269144"
FT DOMAIN 33..107
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
FT DOMAIN 128..202
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 721 AA; 76227 MW; 971AD9EB4527D466 CRC64;
MKLSVLATSV LLAAVSTGAY AYTPGTYTGA IAGQNGPVKV EVTTSADKIL SVKIVDQKET
EGIGSKAVAS LPAEIVKAQS ADVQGVAGAS VSSAAIKKAV QECLNQAQGK KAAPLALKNG
NFEGKAYGNN GWLTVEVTIK DNKIIDIKTP GQRETKYLGD TAIREIGKDV LQYQTLNVDN
IAGATVTSTA LKTAIAQAIE KAGGDIAAFQ KPVSEKIKKV AGITKDSADL IIVGAGGAGL
SAAVTAKDLG VKNVLVLEKM PVIGGNTLRC ASAFNAADPD RQKALPMTET LKEAVVKAIS
EKPVSEEHAK LMADVKAKYE AYLKSGSKTL FDCPEWHALQ TYNGGDKVGQ IPLIRQYSNN
VLDTLHWMQS KGSPVMDRVS QGAGALWQRT HQLDAPAGLG LIDPLYQSAV KQGVNFKLGM
RVQDLILNDK GRVIGVTATD KVGNKYEFTS KDGVILATGG YSQNKEMRRK SAPHLTPEMV
STNQPGATGD GIVIATRHGA DTTGMNYVQV YPLATPGTGA LQGRARKMSG LDDVIDVNKN
GERFVKEDAR RDEFVAAIKK QPGGVVYDIN DSSIVKPLNS FNEDVETLVS IGRIYKADSL
ADLAKQLGMP ADKLEATVAE FNKMVEAKND PKFGRKLFDR PIVKPPFYAT PRAPSIHHTM
GGLQISTNAQ VLDKNGKPIP GLYAAGEVTG GIHGSNRLGG NATADVLTFG RIAAKSAVAH
K
//
