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Database: UniProt
Entry: A0A0A2JLZ4_PENEN
LinkDB: A0A0A2JLZ4_PENEN
Original site: A0A0A2JLZ4_PENEN 
ID   A0A0A2JLZ4_PENEN        Unreviewed;       469 AA.
AC   A0A0A2JLZ4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Alpha-hydroxy acid dehydrogenase, FMN-dependent {ECO:0000313|EMBL:KGO56442.1};
GN   ORFNames=PEX2_080490 {ECO:0000313|EMBL:KGO56442.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO56442.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO56442.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO56442.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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:KGO56442.1}.
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DR   EMBL; JQFZ01000170; KGO56442.1; -; Genomic_DNA.
DR   RefSeq; XP_016598237.1; XM_016745319.1.
DR   AlphaFoldDB; A0A0A2JLZ4; -.
DR   STRING; 27334.A0A0A2JLZ4; -.
DR   GeneID; 27680739; -.
DR   HOGENOM; CLU_020639_1_1_1; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02922; FCB2_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF104; CYTOCHROME B2-LIKE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07020)-RELATED; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          1..59
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          104..459
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
SQ   SEQUENCE   469 AA;  51557 MW;  7CE390DAC366D2F8 CRC64;
     MKLTRQEINR HNNQETCWVV IHGAVYDVTD FLDSHPGGAA VILRCAGKDA TEDFDSVHSL
     ELLSEALPET ALQGYVDPAE LGEPKYKPYA MDEKQSKLDD NSPPPLQSLI NLHDFERIAH
     QRLSATTWAY YSSGADDEIS KLNNALAYQK ISLRPRILRK ITAVNTATVI LGYSTTLPVY
     ISPVGLAKLS HPEGECALAA AAGKEGLVQI LANGSSMPIE QVMKSRTSPK QPIFQQLYVN
     KDIQKSVETV RRAERAGASA IWITVDSPVV GKREMDERLN LTVTATDNGA EEKGVAKIMA
     SSISPFIDWE ILTWLRQLTD LPIVIKGIQC VEDAVLAYQH GVQGIVLTNH GGRSQDTAQA
     PLLTLLEIRK FAPHLIESKM QIFIDGGIRR GTDVLKAIAL GATAVGLGRP FLFSLSGYGK
     DGVRRMIEIL RQEIETNMVF LGVTSLEELR PEMVNTSRLE KHVIGSVKL
//
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