UniProt: A0A2Z6I9H2

Database: UniProt
Entry: A0A2Z6I9H2_9BURK

LinkDB:  A0A2Z6I9H2_9BURK 
Original site:  A0A2Z6I9H2_9BURK

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (15)   

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ID   A0A2Z6I9H2_9BURK        Unreviewed;       639 AA.
AC   A0A2Z6I9H2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=SUTMEG_09860 {ECO:0000313|EMBL:BBF23095.1};
OS   Sutterella megalosphaeroides.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23095.1, ECO:0000313|Proteomes:UP000271003};
RN   [1] {ECO:0000313|EMBL:BBF23095.1, ECO:0000313|Proteomes:UP000271003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23095.1,
RC   ECO:0000313|Proteomes:UP000271003};
RX   PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA   Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT   "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT   Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT   human faeces.";
RL   Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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; AP018786; BBF23095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6I9H2; -.
DR   KEGG; sutt:SUTMEG_09860; -.
DR   Proteomes; UP000271003; 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; 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; 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.
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:UP000271003};
KW   Signal {ECO:0000256|RuleBase:RU366062}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT   CHAIN           31..639
FT                   /note="Urocanate reductase"
FT                   /evidence="ECO:0000256|RuleBase:RU366062"
FT                   /id="PRO_5022264292"
FT   DOMAIN          42..116
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   639 AA;  67462 MW;  CCB20852B125AA46 CRC64;
     MKFKVMRLSA LARATAATVA LVAANGVVSA MTPGTYGATV PARNGAMTVE VTVEANAIKD
     VRVTKHEETP GIGSLAIEAI PARMVELQTA GVDGVTGATV TSDALKRGVE EALKKAGAEP
     GFFAKKSPVA KAAAPLVTQA DVIVVGGGGA GMVAAATAVD GGASVIVLEK MAMLGGNTAR
     SEGNMSAIDP EPEKFLDMTP AVRAIIAKYT DRPACSKEAA ELQKVVKEQL AAHDAAGKKY
     LFDSPELFAL QTIMGGDCKN DPKLVLAMAK NATAAMLWLD EQSDMTWKHV PRHWIDVGIG
     GIYPRGQWPR KADGETPIST YDAYIKPLAE KVTAAGNPIY TSTKVTEIVR DASGRVTGVR
     AEKDGKVVEF KGKNVVLAAG GYGANLEMVK KYNNISVRAT SNQPGATGEV IEEAVKAGAA
     LEGMEWIQIH PHGNPKNGEL ESAIAGRPQD TPYVNVDGVR FIDETGRRDE LSHAILEQPG
     KVVYAIFDRR TIDEGKVRED LMTSALERGF AFKAETLADL ANAAGIKSDA FVKTIDAYNV
     ATRKQDASSL PVTKILFGLT VEKAPFYAVP ITTTIHHTMG GIRINEKTQV LDAKGEPIPG
     LYAAGEVTGG IHGTNRLGRN ALTDLLVFGH IAGQEVSKK
//

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