ID V5ET94_KALBG Unreviewed; 763 AA.
AC V5ET94;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=tRNA dihydrouridine synthase {ECO:0000313|EMBL:EST05209.1};
GN ORFNames=PSEUBRA_SCAF6g00765 {ECO:0000313|EMBL:EST05209.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST05209.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; KI545892; EST05209.1; -; Genomic_DNA.
DR RefSeq; XP_016290198.1; XM_016438895.1.
DR AlphaFoldDB; V5ET94; -.
DR STRING; 1365824.V5ET94; -.
DR GeneID; 27421596; -.
DR eggNOG; KOG2334; Eukaryota.
DR HOGENOM; CLU_375576_0_0_1; -.
DR OMA; WWIESTQ; -.
DR OrthoDB; 276273at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR024624; Pyridox_Oxase_Alr4036_FMN-bd.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR45936; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR PANTHER; PTHR45936:SF1; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF12766; Pyridox_oxase_2; 1.
DR SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 78..355
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT DOMAIN 483..614
FT /note="Pyridoxamine 5'-phosphate oxidase Alr4036 family
FT FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF12766"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 83130 MW; E753C117C8521A3A CRC64;
MPSVAEIRQP PPTTMLPPAK RPKMEASTPI EVEAVAADST SYQDVAPLPE TKESERVDDL
EPIPACTSTL EYRNGIFLAP MVRIGTLPTR LLSLEYGADL VWGPEIVDRA IIGSERKVNP
ATGVVEFLKD HKQIFSCHPM ERPYLVYQLG SADPELAYQA IKTITQADDV AAVDLNCGCP
KPFSTHAGMG ANMLSTPILL CNTLKAMRRA APAHVAVTCK IRLLPTQEKT IELVDKIVRT
GAIECLTVHC RTKDMRPREP ALLHRLREIV DHVNTVAAEM GRTVPVVCNG DVWDATTAPR
IKELTGVTST MIARGAEANP SCFRPEGNLS LPEIIAPKWV RYSIALNNPI GNTKYCMSQL
ALKPAEAGNA KHVSKKQLSA LRMGIAQAKT QEQLAAAFGI DAEEVRAQDV EKEVLKDLRE
ALDARIKQHA TSHSGSGFDG QRLGAVIGNS SGSSGPSSGG QQAGDGHASG PDQKKATSNS
PQPDWKEILA KSIGENIKDE KSILYYAFST VEPPSSVHDA AKPHVRYVVH RGFVNEKRDG
DAEGGVASQN PAFGSSPCLM TTTDVRTPKV QQLTSQSSLR SHGEDGSRGG ECEIAWWIES
TQMQFRISGT VHVLPTKDHP LRSLFPFERL SPPRAPDAMD SDEAFDWDGE RTRIFNKLNA
GLLASFCRPT PGTPHPNAAK LDSAKPKDDT SSPWPLELPQ PGKEENDKQK EQLKESEKNF
ALVVVEPYKV DLVNLAEDTR TIYELVSGEN AATGKWTSRR VVP
//
