ID A0A0Q5EJ17_9MICO Unreviewed; 488 AA.
AC A0A0Q5EJ17;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=NAD-dependent succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KQQ52167.1};
GN ORFNames=ASF68_07295 {ECO:0000313|EMBL:KQQ52167.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52167.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ52167.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52167.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ52167.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52167.1,
RC ECO:0000313|Proteomes:UP000051200};
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|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:KQQ52167.1}.
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DR EMBL; LMOB01000001; KQQ52167.1; -; Genomic_DNA.
DR RefSeq; WP_056008740.1; NZ_LMOB01000001.1.
DR AlphaFoldDB; A0A0Q5EJ17; -.
DR STRING; 1736333.ASF68_07295; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000051200; 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; cd07103; ALDH_F5_SSADH_GabD; 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 PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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:UP000051200}.
FT DOMAIN 23..481
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 51651 MW; 9AB4B11961C012E2 CRC64;
MTDARETELL SKVPSGLFIG GVWRDASDGG TLTVSDPSTG DVIKTIADAS VADGTAALDA
AVAAQDDWAA TAPRTRSNIL RKAFDLLQER RDEFALLMTL EMGKPLAEAN GEVTYGGEFL
RWFSEEAVRI SGRYGSNPEG TGMMTVSQHP VGPCFLITPW NFPLAMATRK IAPALAAGCT
VVVKPAELTP LTTLHFVKLL EDAGLPAGVV NVITTASSSA VSAPIIADPR LRKLSFTGST
PVGQKLIEQS AKNVLRTSME LGGNAPFVVF EDADLDKAVD GAMAAKFRNI GQACTAANRF
IVHRDVADEF AKRVTERVRA FRIGRGTEDG VTIGPLIDDR AVTKAKTLVA DAVGRGAQVL
TGGEAVKGAG TFFQPTVVTG VVPGSDILRE EIFGPVLAIV PFDDEDDAVR LANDTEYGLV
SYVFTTDLAR GQRMIGRLET GMMGLNVGVI SNAAAPFGGV KQSGIGREGG LEGIHEYLYP
KYTMTPID
//