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Database: UniProt
Entry: F0EFK5_ENTCA
LinkDB: F0EFK5_ENTCA
Original site: F0EFK5_ENTCA 
ID   F0EFK5_ENTCA            Unreviewed;       808 AA.
AC   F0EFK5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=HMPREF9087_0507 {ECO:0000313|EMBL:EGC71130.1};
OS   Enterococcus casseliflavus ATCC 12755.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=888066 {ECO:0000313|EMBL:EGC71130.1, ECO:0000313|Proteomes:UP000004835};
RN   [1] {ECO:0000313|EMBL:EGC71130.1, ECO:0000313|Proteomes:UP000004835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12755 {ECO:0000313|EMBL:EGC71130.1,
RC   ECO:0000313|Proteomes:UP000004835};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-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:EGC71130.1}.
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DR   EMBL; AEWT01000002; EGC71130.1; -; Genomic_DNA.
DR   RefSeq; WP_005232825.1; NZ_GL872323.1.
DR   AlphaFoldDB; F0EFK5; -.
DR   HOGENOM; CLU_011398_4_0_9; -.
DR   Proteomes; UP000004835; 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|RuleBase:RU366062};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU366062};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366062}.
FT   DOMAIN          201..275
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   808 AA;  87567 MW;  AE428FD5C017A943 CRC64;
     MKFVGLIGTN AKKSTNRQLV AFMQREFAAL AEIELLEIKD VPMFNETQDQ TNSEVIQRLN
     SKILAADGVI IATPEHNHSI PSALKSVLEW LSFNLHPFDG KPVMIVGASY DVQGSSRAQL
     HLRQILDAPG VNATVMPGNE FLLGRAHQAF DEQGNLKDQR TIDFLESCFR KFVRFTEVAN
     LLNVPEEVVY EPGEYTVTAL GHNGDLPMVV KLSEERIEAI DIDTSGESEG IADVVFVRIP
     QEIIEGQTLN VDAISGASVT SNGVVDGVAK AVKMAGANPD VLRKRPKAAS ALQTEDETYT
     TDVVVVGGGG AGLSAAASVL QANKDVILVE KFPAIGGNTV RTGGPMNAAD PKWQNGFSAL
     PGERSALEEV LTIDEQDIDA EYLPDFKALK AQITAYLSET TPEKEYLFDS ALWHRIQTYL
     GGKRKDLNGQ PIYGKYELVK ILTDQALASV KWLEEIGVEF DMNNVDMPVG AKWRRGHKPV
     KNEGYAFVSA LHQFVKEHGG TILTDTPVKE LLIEDGKVTG IIGEGRNGQK ITIHAKAVIL
     ASGGFGANTK MLKQYNTYWT EIEDDIKTSN SPAITGDGIK LGESAGADLV GMGFSQMMPV
     SDPNTGALFS GLQVPPANFV MVNQKGERFV NEYESRDVLT QAAIDNGGLF YLIADEEIKK
     TAYNTSQEKI DKQVAAGTLF RSETLAGLAE QINVDPTVLE ATVAKYNSYV DAGKDPEFGK
     DVFDLKVEKA PFYATPRKPA VHHTMGGLKI DPQTHVLTKE DQIIEGLYAA GEVAGGIHAG
     NRLGGNSLTD IFTFGRIAGK TAVAEHLE
//
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