ID A0A0F0IGW6_ASPPU Unreviewed; 1320 AA.
AC A0A0F0IGW6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:KJK65977.1};
GN ORFNames=P875_00021939 {ECO:0000313|EMBL:KJK65977.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK65977.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK65977.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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:KJK65977.1}.
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DR EMBL; JZEE01000326; KJK65977.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0IGW6; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd07102; ALDH_EDX86601; 1.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024775; DinB-like.
DR InterPro; IPR019257; MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR NCBIfam; TIGR03439; methyl_EasF; 1.
DR PANTHER; PTHR43397; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR43397:SF1; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 2.
DR Pfam; PF10017; Methyltransf_33; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..331
FT /note="Histidine-specific methyltransferase SAM-dependent"
FT /evidence="ECO:0000259|Pfam:PF10017"
FT DOMAIN 362..492
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 554..671
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT DOMAIN 769..841
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT DOMAIN 853..1312
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT COILED 901..928
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 1086
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 1320 AA; 148133 MW; F57268F7DB10B3DE CRC64;
MSPLALSPKT VDIVNIFQND VEFSLVNEIH KGISPPAGVR KSMPTMLLYD ANGLKLFENI
TYVKEYYLTN AEIEVLETNS RRIVERIPDN AQLLELGSGN LRKIEILLRE FERVGKRVDY
YALDLSLSEL QRTFAEVSID DYTHVGLHGL HGTYDDAVTW LNSPENRKRP TVIMSMGSSL
GNFDRPGAAK FLSQYASLLG PSDMMIIGLD GCKDPGKVYR AYNDSEGVTR QFYENGLVHA
NVVLGYEAFK PDEWEVVTDY DTVEGRHWAA YSPKKDVTIN KVLLKKGEKL FFEEAYKYGP
EERDQLWRDA KLIQSTEMGN GSDDYHLHLL TSATLNLPTS PSQYAAHPIP SFEEWQSLWT
AWDNATKAMV PREELLSKPI KLRNSLIFYL GHIPTFLDIH LTRALRGKLT EPKSYKLIFE
RGIDPDVDDP EKCHSHSEIP DEWPALDDIL DYQERVRSRV RSIYQIEGLA ENRILGEALW
IGFEHEVMHL ETFLYMLIQS ERILPPPATE RPDFKKLYQE ARRSMKANEW FSVPEQTLTI
GLDGADTNDV PPTTYGWDNE KPARTVTVPA FEAQGRPITN GEYAKYLQAN QSRRRPASWV
LTHSDEDYAI PMAVNGSSVG ATQDFMSNFA VRTVFGPVPL EFAQDWPVMA SYDELAEYAE
WVGCRIPTFE ETRSIYLHSA LLKERGGVDH NGEPNGHSLN GDLNGVNGNG YSKINPGKPR
KPDHQPVQYP SRDALPVFLD LHGLNVGFKH WHPTPVIQNG DRLAGQGELG GAWEWTSTPL
APHDGFKAME IYPGYTSDFF DGKHNIILGG SWATHPRVAG RTTFVNWYQH NYPYTWAGAR
LRLQTSGFNM SLETITTISP STNQPVVTRT GVTSEDLQRI PEVAQEAFRS FSRSTTLRQR
QEIVTRALDV LEKKKDELAR ELTEQMGRPI AYTGVEVLTA IKRSRYLTKI SDSVLGEEGV
VPGEEEKGFR RYIKRKPVGV AFIIFAWNYP YLILVNSLIP AILAGNAVIL KPSPQTPTIV
EQFAAAFAEA GLPQNVIQYF HCGSPTLLET IVRSPLVNHV CFTGSVAGGL AVQKAASDRI
VNVGLELGGK DPAYVRDDVD AAWAAEEVVD GAIFNSGQSC CAIERVYVHK NIYDTFVEEV
KKVLSKYRVG DPFDKQTQVG PVISKRAKDT IQAHVADAIQ KGAKDETPAN ETFENFPADG
NYVKPTLLTG VNHDMIVMTE ETFGPIIPVM KVNSDEEAIK LMNSSEFGLT ASVWTKDVAK
AEELVEQVEV GTVFINRSDY PSPDLAWTGW KNSGRGVTLS RFGFEQFVKL KSHHIKAYPK
//
