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Database: UniProt
Entry: A0A0Q8EGC7_9ACTN
LinkDB: A0A0Q8EGC7_9ACTN
Original site: A0A0Q8EGC7_9ACTN 
ID   A0A0Q8EGC7_9ACTN        Unreviewed;       460 AA.
AC   A0A0Q8EGC7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=ASD81_09910 {ECO:0000313|EMBL:KRA38881.1};
OS   Nocardioides sp. Root614.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA38881.1, ECO:0000313|Proteomes:UP000051699};
RN   [1] {ECO:0000313|EMBL:KRA38881.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA38881.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA38881.1, ECO:0000313|Proteomes:UP000051699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root614 {ECO:0000313|EMBL:KRA38881.1,
RC   ECO:0000313|Proteomes:UP000051699};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
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:KRA38881.1}.
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DR   EMBL; LMGV01000001; KRA38881.1; -; Genomic_DNA.
DR   RefSeq; WP_056709668.1; NZ_LMGV01000001.1.
DR   AlphaFoldDB; A0A0Q8EGC7; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000051699; 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   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07087; ALDH_F3-13-14_CALDH-like; 1.
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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051699}.
FT   DOMAIN          4..430
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        212
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   460 AA;  49642 MW;  8DE0EFB569D32532 CRC64;
     MSTEPAETLV ARLRETFDSG RTRDLDWRRD QLGVLARMLR ENEEALLAAL AEDLGKPRFE
     AWAGDVASSA SEADHLRKHL GSWAKDSSAR LPLPFLPGRA SIRHEPRGVV LVIAPWNYPV
     YLLATPLAAA LAAGNAVVCK PSELAPATSA LVTKLAGEYL DPSAVAFVEG GVEDTTALLE
     QKFDHILYTG NGTVGRIVAS AAARHLTPTT LELGGKSPAI VDRDANLKQA ASRIAFAKWS
     NAGQTCIAVD HVWVHHDVHD ELVERLATEV RERYGDDPKQ SPDFGRIVNE RHTARIAGLI
     DAGGYDEVAV GGDVDLAGRY VAPTVLTGVK PDAAVMGEEI FGPVLPVLGF ADISEPIAHI
     NKGDHPLALY VFSRHNADRV LGATTSGGAC VNDTMMQVFP PSLPFGGVGE SGYGAYHGKW
     GFETFSHRRA VYRRPGFFVE PALAKAPYTD LKQRLARFVY
//
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