ID H3KEX9_9BURK Unreviewed; 586 AA.
AC H3KEX9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=HMPREF9440_01294 {ECO:0000313|EMBL:EHY31324.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31324.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY31324.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31324.1,
RC ECO:0000313|Proteomes:UP000004956};
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 (NOV-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:EHY31324.1}.
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DR EMBL; AFBQ01000179; EHY31324.1; -; Genomic_DNA.
DR RefSeq; WP_008542188.1; NZ_JH604957.1.
DR AlphaFoldDB; H3KEX9; -.
DR STRING; 762967.HMPREF9440_01294; -.
DR PATRIC; fig|762967.3.peg.1017; -.
DR HOGENOM; CLU_011398_4_0_4; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000004956; 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.
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:UP000004956};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 24..586
FT /note="Urocanate reductase"
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5022260218"
FT DOMAIN 34..108
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 586 AA; 61948 MW; 036A727138DFAB46 CRC64;
MHQRTTIAAA LTAALALSTT VFAAPVTTEG TATGRHGDLT VAVTFDGGKI RKIDIVKESE
NPILAGKVYT EMRDAMVAAN SVEVDAVTGA TLTSNALRSA VAAASEKAGV KLAAAPVVVA
RKARVPENLV YDVVVIGAGG AGFAAAVSAH DAGAKVVMLE KMPTVGGNSL ISGAEYAAAD
NWVQRKLGIT NDSVELHFQD TMKGGDNLGD PAVVRTMVEG ALPTARWLVD TIGVEFQEDN
VFHFGGHSVK RSLIPKGATG AEFITKFMAA VEKRSIPIYT DTKATELVKD ASGRVVGVKA
TLEGKDYTFE ANRGVIIATG GFAANVEMRT EANPFYGAGF KTTNSPAAMG DGIRMGVAAG
GVAVNMDQIQ TYPMCDPVSG AIELIDDARF EGAILINQEG KRFVEELERR DVMSKAILEQ
TGKYCYALFN EAVEKRSHAI THHQDEVEVF TKTGILKTGK TLDEVAAAFD IPVENLKATV
ARVNEAAKTG KDPDFNYRGK FSDLSTGPYW IYRGVPSVHH TMGGLKIDTK AHVLDKNGKP
VPGLWAAGEV TGSTHGSNRL GSNAYTDIMV FGRIAGEEAA KAEPVK
//
