ID A0A446BLW8_9PEZI Unreviewed; 481 AA.
AC A0A446BLW8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=50c7a862-ce59-48e8-b46c-a0b45184768d {ECO:0000313|EMBL:SPQ23492.1};
GN ORFNames=TT172_LOCUS5911 {ECO:0000313|EMBL:SPQ23492.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ23492.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ23492.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUZ01000010; SPQ23492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A446BLW8; -.
DR Proteomes; UP000289323; 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; PTHR11699:SF204; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-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 20..474
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 481 AA; 51571 MW; 5D33AA0999CE4A60 CRC64;
MANGTPIRPR MLINGELVEA SDGKTFPVYN PATQELSAEG DADDTNAAVA AAKAAFPAWS
AMGGAKRAVY MKKLAALLRE NKDELARLDA IAMGMPVSTH HYAMTAATHF DHYSEAWGTI
QGQASVNTPG FVTMTLRQPY GVVAVIIPWN VPCHFLATKS APALIAGNTV VLKSSEKAPL
AVARIAELVK EAGFPPGVFN IISGHGIPSG QILSRHMDVR ALSFTGSCRT GKLIQEEAAR
TNLKKVILEL GGKSPAIVFE DADLDKAAAQ TQFSIQSNSG QVCMANSRVY VQKSIAPQFI
EAFKTKFAAA RAGDPLDRNT NHGPQADAVQ YRNVLSYIED GKKHGTLALG GHGKLESTNG
FFIEPTVFLN TPETARITKE EVFGPVVVIN TFETEAEAIA KANDTEFGLY AAVFTRDVSR
AMRVAKALES GYVAINCTSP QTAHDLPFGG YKSSGQGREG ILYSMSNFLE TKSIIIKVEE
E
//