UniProt: A0A0A8B6T8

Database: UniProt
Entry: A0A0A8B6T8_9ACTN

LinkDB:  A0A0A8B6T8_9ACTN 
Original site:  A0A0A8B6T8_9ACTN

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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 (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   A0A0A8B6T8_9ACTN        Unreviewed;       618 AA.
AC   A0A0A8B6T8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=JI75_07510 {ECO:0000313|EMBL:AJC12533.1};
OS   Berryella intestinalis.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Berryella.
OX   NCBI_TaxID=1531429 {ECO:0000313|EMBL:AJC12533.1, ECO:0000313|Proteomes:UP000031121};
RN   [1] {ECO:0000313|Proteomes:UP000031121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-1-3 {ECO:0000313|Proteomes:UP000031121};
RA   Looft T., Bayles D.O., Stanton T.B.;
RT   "Coriobacteriaceae sp. complete genome.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJC12533.1, ECO:0000313|Proteomes:UP000031121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-1-3 {ECO:0000313|EMBL:AJC12533.1,
RC   ECO:0000313|Proteomes:UP000031121};
RX   PubMed=26450725;
RA   Looft T., Bayles D.O., Alt D.P., Stanton T.B.;
RT   "Complete Genome Sequence of Coriobacteriaceae Strain 68-1-3, a Novel
RT   Mucus-Degrading Isolate from the Swine Intestinal Tract.";
RL   Genome Announc. 3:e01143-15(2015).
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; CP009302; AJC12533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8B6T8; -.
DR   STRING; 1531429.JI75_07510; -.
DR   KEGG; cbac:JI75_07510; -.
DR   HOGENOM; CLU_011398_4_0_11; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000031121; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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   InterPro; IPR006311; TAT_signal.
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   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.
DR   PROSITE; PS51318; TAT; 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:UP000031121}.
FT   DOMAIN          58..132
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   618 AA;  64395 MW;  8E753C4F13C1C954 CRC64;
     MTDRNKGRAL DRRTFLKGTV ALGVYGGLMG AGLSACSPAK SAAPTAWKAG TYTANVTGHN
     APFTMGVTFS DSAITAIDLG ANQESLGVGA AALKELSDKA MLYQSSNLDA VTGATLSSMC
     FQQGLKECSD QAGASKDLAK AAGPEDTIES AYSADVCVIG AGGAGLTAAI SAVQAGAKVV
     VVEKCGITGG STNVSEGALN AVDPERQSKQ NIDDSVDKFY DTTFKGGHEQ GTPELIRYLV
     DNALDSVHWL ESLGVQFKEK VGSATGSLGE RSHYPATPSG NTYIRAFQAF AEAHADQMTI
     LHETQVTSLI VENGAVAGIK GLHRKKDEIT VKAKAVVVAT GGFGANVEYR QKVNTGVWAD
     VKLDDTIGCT NIKPCAQGEG LKLAEDAGAQ LVGLPDIQLH PCGTPGTGLM EDIRTSGRNR
     IFVNKDGERF VNEGAERDTL CKAIFAQPDS TYWIVVNKVR YPSETEPDAN GATIENMLAL
     EHIVKGESVK DLAAACGMDP EKLQASIDGY NKTVSGQAED PFGFKANNTA DKELTEGPWY
     ACRKVPTVHH TMGGIRIDVD TRALDANGSA VQGLFACGEC TGGIHGSNRL GGNAIADCVT
     FGRAAGKNAA EAALATGN
//

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