ID G7X782_ASPKW Unreviewed; 1010 AA.
AC G7X782;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:GAA83104.1};
GN ORFNames=AKAW_01219 {ECO:0000313|EMBL:GAA83104.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA83104.1};
RN [1] {ECO:0000313|EMBL:GAA83104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA83104.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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DR EMBL; DF126448; GAA83104.1; -; Genomic_DNA.
DR AlphaFoldDB; G7X782; -.
DR STRING; 1033177.G7X782; -.
DR VEuPathDB; FungiDB:AKAW_01219; -.
DR eggNOG; KOG0254; Eukaryota.
DR eggNOG; KOG2456; Eukaryota.
DR InParanoid; G7X782; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07135; ALDH_F14-YMR110C; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..460
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 1010 AA; 111458 MW; 6ECF9B4ACFFA1946 CRC64;
MASLRNLQSM RHAFTWNMLI AYAIIATSVF SYGFDDAVYS TIQTMDSFEK QFGTYDSSTG
EYGFSTQHLA FLNSLGLPAK AAGTFIGWAI GEYYGRRTCF IGMQLMCIIG ISVSYSATTF
GQILAGRMIV QCFIGWEDWL VPMFLGEICP TVVRGATVVV YVFAHIFGSF ICAIITYETA
KLEGNAAWKI PIGVMWTFPC FILLCSWLVP ESPRWLVRKN KIQAATKQLE YLNKGKDVDV
AGEVAFLQAA VEANAQTKGS WAELLQGTNR RRTMIAMMTA AFNQLTGQSF VSQYGSLFVK
SLKVMNPFAF TLGSRGISTM GPLVTFSLVD TTGRRPIYLI GGTMTTALLM ICGGLGTGTI
TDGKKRGVCG VLMMYGLFYI MSFGSISVIT GAETPHLRLR DKTSVVAWLI RIVCDFAVSY
SLPYLLKAPY ADLQSKVGFI YGSLAAVGVV CGYFFLPELT GRSLEELEDM WQRRIPARKF
ADWESSCIGS IGAKVTEMEG ETEDAAYASV RAAFASGRTK SKDWRRHQLK RAWWMVEDNK
NRILDALRAD LNKHPLEALL GEITGLQNDI LRTLEKLDEW TKDEKPTRWD PINFLGGTVV
RQEPLGVSLI IGAWNFPFML TLQPLIAAIA AGCAVVLKPS DVAQASQNLL MEIIPMYMDR
DAITCVSAGP SEMKHILESR FDHIFYTGSA NVAKIIYAAA AKHLTPVTLE LGGQGPAIVA
PSANIDLAAK HIAWAKFSNA GQICINVNHV LIDPSIREAF VTKLIHYFDE FTGGPDNKPD
YYSRIVNERN FDRLESLLDR TTGKVIHGGI RDRQNRYFGP TIVVDVSPED SLLSEELFGP
ILPIIDADLD TAISFTRSIE HPLALYAFTT VESEKKRIQD ETASGGVTFN DCFLHAAALD
APFGGVGNSG AGCYHGKYGI LAFSHLRTYT NAIPTWLEGV MGARYPPYSE TNMRKLSPPV
KPPFDREGND TTSRSKILSA AATLAVLGIS VWMFGAREKL PPYGRNWLRK
//
