ID A0A1F5LXD2_9EURO Unreviewed; 899 AA.
AC A0A1F5LXD2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FMN hydroxy acid dehydrogenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENARI_c001G08923 {ECO:0000313|EMBL:OGE57812.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE57812.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE57812.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE57812.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE57812.1}.
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DR EMBL; LXJU01000001; OGE57812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LXD2; -.
DR STRING; 1835702.A0A1F5LXD2; -.
DR OrthoDB; 2476752at2759; -.
DR Proteomes; UP000177622; 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 CDD; cd00118; LysM; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.350.10; LysM domain; 4.
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; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
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; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF54106; LysM domain; 3.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
DR PROSITE; PS51782; LYSM; 4.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..899
FT /note="FMN hydroxy acid dehydrogenase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519986"
FT DOMAIN 225..270
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 275..321
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 365..411
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 446..492
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 530..892
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 498..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 96880 MW; 454444580E011330 CRC64;
MKFTVIFVIT YFASAFAQID LYEYGTNATA FISDGCTSAL RKELNCDPYL LTLSMSDYFG
PVGNQTFQDQ LCDEGCGSAL ETYHSSVKQQ CAGDVEPWDG VPAVWAGDVL WSTWNRTCLK
DPKTNTYCTD AIGDIQAALG DIDTALAAVS KDQLCSTCVL NLIQQMQKTA YSNYDEQLVD
EYVKIQDTCN TGALPTEVQP PATNMTAIPG IDYSTPSNIS CLSGNFYSAK SGDDMQSIAK
AQKVPTGPLR TLNGIFPDGS NLLAGQNLCL PRACPVYLVQ DGDNCNSIAD SYGLTIADLI
SYNPSINRAC SNLNSGDNVC VGASGQLYTP TTIPGATATK TAQYAASTVA AAGPTGYGTT
KECGGYYPAA DGDDCEQISL IYSISLDLFL AINPAINAAC SNLFPGLYYC VYPTANWNAT
TNGTTTSTYV TPPAPTPTGT TSNCYTWHTI VDKDSCSLLQ NVYGITFAQL RTWNPQLNEE
CSNLLLDAAY CVRGDTDTTT TSTTETAGTT TSKTTTTADQ PTQTSVPAPG PTQDGVPKNC
NSWVMQKEVL NQGLDFFNSG ATNQVTLHDN YSAYRKYRLL PRVLKDVSQV DTGISLFGRD
ILFPLCASPT GLQVLAHPDG ELATSRACAK AGVNMGVSSY TGYPVEQITE AGNEVGPVNH
VMQLYTLNDK AKQERIVRRA EAAGCKAIFL TADSPVLGVR WNEWRNGFKP PPGVAYPMYE
KTSDEIQAQS HDDGFTSTNS DSHSWATEIP WLRSITKMEI WIKGVLTPED VEIAVEYGCD
GVIISNHGGR QLDETPATID ALPACAKVAR GRIRIHIDGG IRSGADIFKA LALGAECCWV
GRPVLWGLAH DGQQGVELMF KILYDDFKRC MQLTGCKSVS EIRPELLAIV NAYGPLARL
//
