ID G3XZZ8_ASPNA Unreviewed; 513 AA.
AC G3XZZ8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=ASPNIDRAFT_53357 {ECO:0000313|EMBL:EHA23709.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA23709.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA23709.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA23709.1}.
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DR EMBL; ACJE01000009; EHA23709.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XZZ8; -.
DR STRING; 380704.G3XZZ8; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43720:SF3; ALDEHYDE DEHYDROGENASE ALDH (AFU_ORTHOLOGUE AFUA_8G02310)-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 31..505
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 513 AA; 55813 MW; 9162C3F7D39F19BE CRC64;
MADSLFVDIT TPNGRQYQQP TGLFINNEFR PSSSGQTIVS LDPATDKPIA TVHAATAEDV
DAAVQAAKAA LSHPSWKLLP ATERGQLMGR LADLMEENRA LFAAIDAWDN GSYTHHPHRY
ADTDLANRKT LPPITTIRYY SGWADKTFGQ TISTTPQKFA YTIRQPIGVV GQIIPWNYPL
SMATWKLGPA LACGNTVVIK AAEQTPLSIL VLATLIKKAG FPPGVVNVIN GYGKEAGAAL
VQHPLVDKIA FTGSTATARE IIKMAAGTLK NITLETGGKS PLIVFPDADL EQAVKWSHFG
IMSNKGEICT ATSRIFVHRS ILASFLEKFK KEIETTSKIG DQWDENTYQG PQVTRAQYER
VLSYIETAKK EGATLVTGGK AYTPKDEKNA KGYFVEPTVF TDVTDDMRIC QEEVFGPVVV
ILPFDSEEES VRRANDTTYG LGAAVFTTDL ERAHRVAADI EAGMVWINSS QDCDPRVPFG
GVKQSGIGRE LGEAGLEAYS QVKAVHVNMG SRL
//
