ID A0A120I990_9LACT Unreviewed; 804 AA.
AC A0A120I990;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Urocanate reductase {ECO:0000256|RuleBase:RU366062};
DE EC=1.3.99.33 {ECO:0000256|RuleBase:RU366062};
GN ORFNames=AWM72_05045 {ECO:0000313|EMBL:AMB94164.1}, CYJ28_03860
GN {ECO:0000313|EMBL:PKZ22255.1};
OS Aerococcus sanguinicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94164.1, ECO:0000313|Proteomes:UP000069912};
RN [1] {ECO:0000313|EMBL:AMB94164.1, ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|EMBL:AMB94164.1,
RC ECO:0000313|Proteomes:UP000069912};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PKZ22255.1, ECO:0000313|Proteomes:UP000234239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0139 {ECO:0000313|EMBL:PKZ22255.1,
RC ECO:0000313|Proteomes:UP000234239};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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}.
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DR EMBL; CP014160; AMB94164.1; -; Genomic_DNA.
DR EMBL; PKGY01000002; PKZ22255.1; -; Genomic_DNA.
DR RefSeq; WP_067974197.1; NZ_PKGY01000002.1.
DR AlphaFoldDB; A0A120I990; -.
DR GeneID; 69593678; -.
DR KEGG; asan:AWM72_05045; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000069912; Chromosome.
DR Proteomes; UP000234239; 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; 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; 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:UP000069912}.
FT DOMAIN 200..274
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
SQ SEQUENCE 804 AA; 88073 MW; 4179D8D07B97128A CRC64;
MKFVGIVGTN AEFSYNRKLL EFMADYYEED TIEVLDIDRV PMFNETKDQT DTAPIQELKE
KIEAADGVII ATPEHNHSIP SALKSVIEWL SYKIHPLDGK PVMIVGASYS VQGSSRSQLH
LRQILDAPGV NAIVMPGNEF LLGRAHEAFD EDGKLKDKRT VQFLSSCFRK FKRFTEVAEI
LNQPEEVNFK PGDYHVSAVG HNGDLPMVVT FSEDRIEAID IDTEGETEGI ADLVFTRLPE
EIIDGQTLNV DVVSGASVTS NGVVDGVADA VYQAGSDPEI LKKRPKVSES MQLDPVEKTV
DVAVIGSGGA GLAAAIAALD KGASTLVLEK FPVIGGNTVR TGGQINAADP EWQHQFKAIH
GERATLEKIY NTPEDEIAEE YREDFRALKE ELDQYFKDLD EGKSYLFDSI HLHTIQTYIG
GKRMDLDGNE IHSDIELIHY LTKNALPTID WLKEKGVTFD EHMVAEPVGA LWRRAREPQA
SEGFGYIDPL TTYIEDHGGQ IMTDTKADRF IVEDGKIVGI QATGRYDQKV TIHVNKGVVI
ATGGFGANIE MIKKYDNYWG NLPESIPTTN SPALTGDGIE MGQEVGADVV GMGFVQLMPS
ADPITGNIFS GIDCPPSDFI FVNKEGKRFV DEYASRDVLA KALFDQGGVI YNISDAEIAK
TRFNSTDEQL ANDVKKGACF KADTLEDLAK QLDIDPAVFV KTIEDYNSYV DQGYDEEFQK
GAFNHKVIVP PFYATPRSPA THHTMGGLKI DAQTRVLNTQ GQAIEGLYAA GEVAGGVHAG
NRLGGNALAD IFVFGKLAGQ NAAE
//
