ID G0S195_CHATD Unreviewed; 608 AA.
AC G0S195;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN ORFNames=CTHT_0012800 {ECO:0000313|EMBL:EGS22805.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22805.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; GL988039; EGS22805.1; -; Genomic_DNA.
DR RefSeq; XP_006691797.1; XM_006691734.1.
DR AlphaFoldDB; G0S195; -.
DR STRING; 759272.G0S195; -.
DR GeneID; 18255318; -.
DR KEGG; cthr:CTHT_0012800; -.
DR eggNOG; KOG2454; Eukaryota.
DR HOGENOM; CLU_005391_1_0_1; -.
DR OMA; ILMRGTF; -.
DR OrthoDB; 5743at2759; -.
DR Proteomes; UP000008066; 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 CDD; cd07098; ALDH_F15-22; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 83..550
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 608 AA; 66205 MW; 07E67A37655C319B CRC64;
MASTVVDTVL QLLDQLPPII QQFSPKNSPE TYLTVLAAIV LAYSNWLLFQ SLSNRPIPYK
VSPPERPEKP EILEKPSIKV EGSNTIRCYA PATGELLGYV EPATPETIDR AIEEAHEAQK
KWANTSFNER RAVLRTLLQH VLDNQEQICR IACLDSGKTM VDAQLGEVLV TVEKLQWTIK
HGEKALVPER RPTNLLMTYK RNTVRYEPLG VVSALVSWNY PFHNLIGPVI SAIFSGNGIL
VKVSEQTAWS SQYFTKLIRG ALIAHGHDPR LVQTVVCWPE VAGHITSHPR ISHITFIGSR
PVCHKVAASA AKALIPVVAE LGGKDASIIL DTVSKSDLPR VVEILMRGSF QASGQNCIGI
ERIIAAPGIY DKLVSLLEPR VRALRLGQNA DVGAMISDNN FARLEGLIAE AVSRGARLLV
GGKRYAHPDY PNGHYFSPTL LVDVTPDMAI ANEECFAPIM VIMRAPSPSA EDILAVANAP
DFGLGSSVFG ADSDPRIPKI VRGIKAGMIS VNDFAATYAV QLPFGGVAGS GYGRFAGEEG
LRGLCNVKAV CEDRMSWLGV RTAIPPPMRY PVVDQERSWR FAKGIVEVGY AMGLWGKLAG
VLGIVKNS
//
