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Database: UniProt
Entry: A0A0Q5DER1_9BURK
LinkDB: A0A0Q5DER1_9BURK
Original site: A0A0Q5DER1_9BURK 
ID   A0A0Q5DER1_9BURK        Unreviewed;       511 AA.
AC   A0A0Q5DER1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN   ORFNames=ASF61_03935 {ECO:0000313|EMBL:KQQ39971.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ39971.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ39971.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ39971.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ39971.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ39971.1};
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:KQQ39971.1}.
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DR   EMBL; LMNW01000012; KQQ39971.1; -; Genomic_DNA.
DR   RefSeq; WP_056153730.1; NZ_LMNW01000012.1.
DR   AlphaFoldDB; A0A0Q5DER1; -.
DR   STRING; 1736266.ASF61_03935; -.
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; cd07112; ALDH_GABALDH-PuuC; 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; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR11699:SF291; NADP_NAD-DEPENDENT ALDEHYDE DEHYDROGENASE PUUC; 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          29..495
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   511 AA;  54102 MW;  4BE2FF99C716CCB2 CRC64;
     MDKDYAYYRQ QADLIVPRLE TRALIGGRFV DAASGARLDT VNPATGRMIA AIASCDQADV
     DLAVRAARLA FDRGDWSRAA PKHRKKVLLR LADLVEENLE TLAILESLDA GKPVRDTLGT
     DLPDMIESLR WHAEAADKLY DQVAPTAPDV VAMVVREPLG VVGAVLPWNF PLYLAGWKIG
     PALASGNSLI IKPAEQTSLT ALMLGRLALE AGIPDGVLQV VPGTGETVGR ALGLHGDIDG
     VSFTGSGEVG RLFLQYAAQS NLKRVVLECG GKSPALVLPD AVDLPRVADQ IALGALFCQG
     ENCSAGSRLI VHRARKDELL EEVKRAFDAW RVGDPLDPAT RVGALIEPGH MARVLGYIAG
     AREQGAQLVH GGAQVRRETG GSFVEPTIFD NVQASMTIAR EEVFGPVLAV TAYDALAQGV
     AIANDTSYGL AASVYTGSLD AAHGVARAIR AGTVSVNCFS EGDTGVPFGG YKESGFGGRE
     KSLLAHDQYT ETKTIWIQLG AAGSTESKEG R
//
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