UniProt: U2NIP4

Database: UniProt
Entry: U2NIP4_9CLOT

LinkDB:  U2NIP4_9CLOT 
Original site:  U2NIP4_9CLOT

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (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 (18)   

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ID   U2NIP4_9CLOT            Unreviewed;       807 AA.
AC   U2NIP4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=CINTURNW_3495 {ECO:0000313|EMBL:ERK29008.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK29008.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK29008.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK29008.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT   Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(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}.
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:ERK29008.1}.
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DR   EMBL; APJA01000022; ERK29008.1; -; Genomic_DNA.
DR   RefSeq; WP_021803444.1; NZ_KI273145.1.
DR   AlphaFoldDB; U2NIP4; -.
DR   STRING; 1294142.CINTURNW_3495; -.
DR   PATRIC; fig|1294142.3.peg.3644; -.
DR   eggNOG; COG0431; Bacteria.
DR   eggNOG; COG1053; Bacteria.
DR   eggNOG; COG3976; Bacteria.
DR   HOGENOM; CLU_011398_4_0_9; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000016721; 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; 3.40.50.360; -; 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; 2.
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:UP000016721}.
FT   DOMAIN          201..275
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   807 AA;  88114 MW;  185DDD6C95798201 CRC64;
     MKFIAIVGTS AKKSYNRKLL QFMKKYFDSK AEIEILEITD VPMFNQSDNQ SSSEVIQMFN
     NKIIASDGVI IATPEYNHSV PSSLKSLIEW LSFDLHPLAG KPVMILGASL DTQGSSRAQL
     HLRQILDAPG VDANVMPGYE FLLGNANKAF DEEGNLNNER TIDFLEICFL RFMRFAKIAN
     QLNEEEEFTF NPGVYEVSAI GHSGSLPMKV SFSENRIESI DINTDGETEG LADVVFVRIP
     DKIIEGQTLN VDALSGASET SNAVLDGVAK AVKLAGVNPD ILKRRPKPAS SLIKEDEEYT
     CDVVVVGGGG AGLSAAATAL QNGSSAIVLE KYPAVGGNTI RSGGPVNAAD PEWQVKFDEN
     PGERHTIEAL LDTDESLIHP EYLDDFHALR KEFSDYKKKF DTQKGHLFDS PLLHRMQTYF
     GGKRTDLNGN AIYGQYDLVK ILTDRALESV KWLEEIGVEY DKSIVFAPVG ALWRRGHKPT
     KSHGSSFILA LTKYVQDNSG KIITDSPVKE FIIEDGEIKG VIATGVNGQK ITVHAKAVVL
     ASGGFGANTK MLKEYNTYWS DIADDIKTTN SYAMTGDGIL LGKTVGAALT GMGFTQMMPV
     ADPETGELFS GVQVPPENFV MVNKEGKRFI NEFSGRDVLT KAAIEQGGLF YLIADDEIKE
     TAANTSQEKL DRQVEAGTLF RADTLEELAV KVGMEPAVLV DTINKYNSYV DAGFDPEFHK
     DTFSLKVEKA PFYATPRKPA VHHTMGGLKI DTKAHVLDEN DNPIKNLYAA GEVAGGIHAG
     NRLGGNALTD IFTFGRIAGK TAVDEMK
//

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