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Database: UniProt
Entry: A0A0R2AEE7_9LACO
LinkDB: A0A0R2AEE7_9LACO
Original site: A0A0R2AEE7_9LACO 
ID   A0A0R2AEE7_9LACO        Unreviewed;       807 AA.
AC   A0A0R2AEE7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE            EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN   ORFNames=FC26_GL002286 {ECO:0000313|EMBL:KRM61068.1};
OS   Paucilactobacillus vaccinostercus DSM 20634.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61068.1, ECO:0000313|Proteomes:UP000051733};
RN   [1] {ECO:0000313|EMBL:KRM61068.1, ECO:0000313|Proteomes:UP000051733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61068.1,
RC   ECO:0000313|Proteomes:UP000051733};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(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}.
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:KRM61068.1}.
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DR   EMBL; AYYY01000043; KRM61068.1; -; Genomic_DNA.
DR   RefSeq; WP_057779521.1; NZ_AYYY01000043.1.
DR   AlphaFoldDB; A0A0R2AEE7; -.
DR   STRING; 1423813.FC26_GL002286; -.
DR   PATRIC; fig|1423813.3.peg.2330; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000051733; 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:UP000051733}.
FT   DOMAIN          200..274
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   807 AA;  87704 MW;  EE69A79572DB928A CRC64;
     MKLIGIVGTN AEKSYNRQLL TFMQRHFADQ AEIEILEIKD VPMFNESADQ NLPIIQTFDQ
     KIIDADGVII STPEHNHSIP SALKSTLEWL SNDVHSFEGK PVMIVGASYH DQGSSRAQLH
     LRQILDAPGI DAIVMPGNEF LLGHAQQAFD EHGDLNNEGT VSFLASCFKK FLRFTNMVKM
     LNVPEDLKVN PGTYDVTAMG HNGKLPMSVE FSEDKIENIE IDTSAETAGI ADVVFEKIPA
     QILSGQTLNV DTVSGASVTS KGVIDGVAEA VKLAGGDPDV LKNRPRPSAK RQVPPVEYET
     DVVVIGAGGA GLTAAASVLQ RGQRVIVAEK FPSVGGNTVR TGGPMNAADP TWQNEFSANP
     GERTTLQGIL NTDEATIDPA YVADFRLLKT QITKYLETTD DDNEYLFDST LFHRIQTYLG
     GKRVDLAGHE IHGQYDLVKI LTDHALESVK WLESIGVEFD QTEVSMPVGA KWRRGHKPLK
     NQGYAYVSAL KTFVEQRDGQ ILTETPAKKL IIEDGEVRGI IAQGPDDQKV IIHASAVILA
     SGGFGANTKM VQQYNTYWQQ IDDDIQTSNS PAITGDGIKL GTSAGADLVG MGFSQMMPVS
     DPETGELFTG LQVPPANFVM VNQQGKRFVN EYEGRDVLSK AAIANGSLFY LIADDKIKET
     AYNTSQEKID QQVEDGTLYR ANTLAELAQQ IHVDPAVLTT TIAHYNSYVD AGTDPEFGKN
     VFDLKVEQAP FYATPRKPAI HHTMGGLRID TQAHVLNEQG TVIPHLFAAG EVAGGIHAGN
     RLGGNSLTDI FTFGRVAGKT AVSENQK
//
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