UniProt: U5MMB3

Database: UniProt
Entry: U5MMB3_CLOSA

LinkDB:  U5MMB3_CLOSA 
Original site:  U5MMB3_CLOSA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   U5MMB3_CLOSA            Unreviewed;       807 AA.
AC   U5MMB3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   Name=urdA {ECO:0000313|EMBL:AGX41909.1};
GN   ORFNames=CLSA_c08970 {ECO:0000313|EMBL:AGX41909.1};
OS   Clostridium saccharobutylicum DSM 13864.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX41909.1, ECO:0000313|Proteomes:UP000017118};
RN   [1] {ECO:0000313|EMBL:AGX41909.1, ECO:0000313|Proteomes:UP000017118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX41909.1};
RX   PubMed=24285650;
RA   Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA   Gottschalk G., Daniel R.;
RT   "Complete Genome Sequence of the Solvent Producer Clostridium
RT   saccharobutylicum NCP262 (DSM 13864).";
RL   Genome Announc. 1:e00997-13(2013).
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; CP006721; AGX41909.1; -; Genomic_DNA.
DR   RefSeq; WP_022744196.1; NZ_AYXL01000004.1.
DR   AlphaFoldDB; U5MMB3; -.
DR   GeneID; 55473430; -.
DR   KEGG; csb:CLSA_c08970; -.
DR   PATRIC; fig|1345695.10.peg.4108; -.
DR   eggNOG; COG0431; Bacteria.
DR   eggNOG; COG1053; Bacteria.
DR   eggNOG; COG3976; Bacteria.
DR   HOGENOM; CLU_011398_4_0_9; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000017118; 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; 3.40.50.360; -; 1.
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; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR005025; FMN_Rdtase-like.
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   Pfam; PF03358; FMN_red; 1.
DR   SMART; SM00900; FMN_bind; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 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:UP000017118}.
FT   DOMAIN          201..275
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   807 AA;  88396 MW;  65E77921816285DD CRC64;
     MKFIAIVGTS AKRSYNRKLL QFMKKYFDLK AEIEILEITD VPMFNQSDNQ SSSEVIQMFN
     DKITASDGVI IATPEYNHSI PSSLKSLIEW LSFDLHPLAG KPVMILGASL DSQGSSRAQL
     HLRQILDAPG VDANVMPGYE FLLGSANKAF DEEGNLNNER TIDFLEICFL RFMRFAKISN
     QLNEEEEFTF KPGVYEVSAI GHSGSLPMKV SFSEDRIESI DINTDGETEG LADVVFVRIP
     DKIIEGQTLN VDALSGASET SNAVLDGVAK AVKLAGVNPD ILKRRPKPAS SLIKEDEEYT
     CDVVVVGGGG AGLSAAATAL QNGSSAIVLE KYPAVGGNTI RSGGPINAAD PEWQIKFEEN
     KGERHTIEEL LDTDESLVHP EYIDDFRALR KEFSEYKKKF ETQKGHLFDS PLLHRMQTYF
     GGKRTDLNGN TIYGQYDLVK ILTDRALESV KWLEDIGVEY DKSIVFAPVG ALWRRGHKPT
     KSHGSSFILA LTKYVQDNSG KIITDSPVKE FIIEDGEIKG VIATGVNGQK ITVHAKAVVL
     ASGGFGANTK MLKEYNTYWS EIADDVKTTN SYAMTGDGIL LGKTVGAALT GMGFTQMMPV
     ADPETGELFS GLQVPPENFV MVNKEGKRFI NEFSGRDVLT KAAIDQGGLF YLIADEEIKK
     TAANTSQEKL DRQVEAGTLF RADTLEELAV KVGMDPAILV DTINKYNSYV DAGFDPEFHK
     DTFSLKVEKA PFYATPRKPA IHHTMGGLKI DTKAHVLDEN DKPIKNLYAA GEVAGGIHAG
     NRLGGNALTD IFTFGRIAGK TAIDEMK
//

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