ID A0A364KQB7_9EURO Unreviewed; 1029 AA.
AC A0A364KQB7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=FMN hydroxy acid dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51349};
GN ORFNames=BHQ10_001766 {ECO:0000313|EMBL:RAO65754.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO65754.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO65754.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO65754.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
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:RAO65754.1}.
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DR EMBL; MIKG01000002; RAO65754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364KQB7; -.
DR STRING; 1196081.A0A364KQB7; -.
DR OrthoDB; 1549204at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR010730; HET.
DR PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR Pfam; PF06985; HET; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
FT DOMAIN 1..364
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 887..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 115853 MW; ACD65B9A611AB37C CRC64;
MGTPILCIDD IRKEAEKKLE KSSTDFFNSG STDQVTVREN STAFAKYRIR PRVLKDVSNA
DTSVTVLGRK IAFPLCVSPA GIQALAHPDG ELATARACAK RGVHMGVSSF SNYTVEEVIA
ASKETGLGRT AHVMQLYTMQ DRALQERVIR RAEAAGCVAI FLTADSPVLG FRYNEWRNDW
RTPAGLAFPM LEKTTEMIQS QTHDESFTVF NSDSHSWAYD IPWLRSKTKM QIWIKGILTA
EDVLLARQYG CDGVLVSNHG GRQLDGTPAT LDALPECIAA ADGKIPVHID GGFRTGADIF
KAIALGAQCC WVGRPAIWGL GYDGEKGVTK TLDILYDEFK RVMQLAGCWL RLITVSDLLN
DDNPTLILSE WRGLDITNPG DSFIPKYATI SHSWAASDEV QRLSEIADRP LRIDLGNDKY
HTISWEGLVQ AAKAAQHLGC VFIWLDLTCV HQNSSEDKKL QIQHMGHVYQ RSVAVIVMPG
GVASAQGVGN TAPWITRAWT LQEATLSPEN VHVLIKEPRW DTTNYDYEYG TTGPTYQIDQ
VDDDLALSKL QNLLSCRKRG LEITRVNKST KVKTRVPFIV RCFGADESLI TALEGVLRGH
TDEMKRSAAW RSIYLRTSTK PQDMVFSVMH LLGVSIKVDY DRTREDLILE LARKTKDLPS
WLDIGEDIPF DARFGLVPAL PIFHPNDMPS YDIDRELVPA NRYTESGTYI HEYDIKIQTS
PTSIFDGDLI CAKIFPITFQ NVSGASITSG DGEKFDFSDV DQKNVTGSHV VVLGEARVYA
LAHLGLMHFG GPQVIFVGRS ERGIWERHGK RAFIPGKFAE NAWRWHLTIG GKPGSEITPL
VLQSIPPFIA RHGFVIHHFF LELNKSLNTS LSRTLFYTQR ATYASTSSSP FRLSSSPKQP
QSQSQPQPTE DEDAYRYEYE AENEGAYYSP YRPKRQWPPD MSKLSPKHQL RLERKYRRRA
ALKYARPRWV KFTKLAQWGI IIFIVIYSLL FMEWGKEGEE HPFEDFRKDF FASINSLFSA
PERPIKKKE
//
