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Database: UniProt
Entry: A0A0Q5D337_9BURK
LinkDB: A0A0Q5D337_9BURK
Original site: A0A0Q5D337_9BURK 
ID   A0A0Q5D337_9BURK        Unreviewed;       506 AA.
AC   A0A0Q5D337;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KQQ39090.1};
GN   ORFNames=ASF61_22360 {ECO:0000313|EMBL:KQQ39090.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ39090.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ39090.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ39090.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ39090.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ39090.1};
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|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:KQQ39090.1}.
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DR   EMBL; LMNW01000018; KQQ39090.1; -; Genomic_DNA.
DR   RefSeq; WP_056155602.1; NZ_LMNW01000018.1.
DR   AlphaFoldDB; A0A0Q5D337; -.
DR   STRING; 1736266.ASF61_22360; -.
DR   OrthoDB; 6187633at2; -.
DR   Proteomes; UP000051032; 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; cd07116; ALDH_ACDHII-AcoD; 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; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          34..493
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   506 AA;  55211 MW;  1B8F18A5837C6762 CRC64;
     MNLADIRTLG VENPFKQRYD NYIGGKFVAP VKGEYFGNVT PITGQVFCEV ARSTAEDVEL
     ALDAAHAAKA AWGKTSQAER ANILNKIADR MEANLALLAT AETIDNGKPI RETTNADLPL
     AVDHFRYFAG CIRAQEGSVA QIDADTYAYH FHEPLGVVGQ IIPWNFPILM AVWKLAPALA
     AGNCVVLKPA EQTPASIMVL VELIGDLLPP GVLNIVNGYG LEAGKPLASN KRIAKIAFTG
     ETGTGRLIMQ YAAQNLIPVT LELGGKSPNI FFADVMDADD AFFDKCLEGF AMFALNQGEV
     CTCPSRVLIQ ESIYEKFIER ALARVAAIKQ GNPLDAGTML GAQASQEQLE KILSYIDIGK
     QEGAEVLAGG ERHVQDGDLK EGYYVRPTVF KGENSMRIFQ EEIFGPVVSV TTFKDEEDAL
     RIANDTLYGL GAGLWTRDGS RAFRVGRAIQ AGRVWTNCYH LYPAHAAFGG YKQSGIGREN
     HKMMLDHYQQ TKNLLVSYSP NALGFF
//
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