ID W5W7T4_9PSEU Unreviewed; 503 AA.
AC W5W7T4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Putative aldehyde dehydrogenase dhaS {ECO:0000313|EMBL:AHH96785.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:AHH96785.1};
GN ORFNames=KALB_3418 {ECO:0000313|EMBL:AHH96785.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH96785.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH96785.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH96785.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007155; AHH96785.1; -; Genomic_DNA.
DR RefSeq; WP_025356906.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W7T4; -.
DR STRING; 1449976.KALB_3418; -.
DR KEGG; kal:KALB_3418; -.
DR PATRIC; fig|1449976.3.peg.3437; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_11; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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: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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT DOMAIN 25..494
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 503 AA; 53618 MW; 3F7EBD090BAC7C29 CRC64;
MTLTVTPHRE AVGLKDGLLH VDGRWRPGRE GRTWTHHHPA TGEAVGSFAV AEAADVDEAV
RAASKAFEAG PWPRTKAGQR IAVLLRYAAL LREHAEELKR LQALDNGVPL SFGGIYATSV
GIAADIFEHH AGWIDKIGGQ TLPAHQGGDH LAMTFREPIG VVAAILPWNA PFVLFAQKLA
PALAAGCTVV LKPSEYATFC VVRMVELLAE AGLPEGVVNL VTGPGDPTGE ALITHPLVDK
ISFTGSRAVG QRIVRASADT MKRVSLELGG KSPAIVFPDA PNIGLAGMTA MGMVTVGLSG
QACVAHTRAL VHRDVYEEFL GAAQMMAGAV TFGDPFDPAV LASPLINERQ LGRVLGFIER
GQQQGARLVT GGERMDGDYG AGNFVTPTIF AEVDNSMEIA REEVFGPVLT VLPFTEEDEA
VRIANDTDYG LGAGIYTADA RRAFRLARRL RAGTIGINGF QLEPHVPFGG FKQSGLGREG
GRSAFEDYTE LKTVLMPLTD EMM
//