ID A0A0Q8QHC7_9ACTN Unreviewed; 494 AA.
AC A0A0Q8QHC7;
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:KRB80478.1};
GN ORFNames=ASE01_03175 {ECO:0000313|EMBL:KRB80478.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB80478.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB80478.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB80478.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB80478.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB80478.1,
RC ECO:0000313|Proteomes:UP000050886};
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:KRB80478.1}.
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; LMIA01000001; KRB80478.1; -; Genomic_DNA.
DR RefSeq; WP_056748519.1; NZ_LMIA01000001.1.
DR AlphaFoldDB; A0A0Q8QHC7; -.
DR STRING; 1736488.ASE01_03175; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000050886; 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:UP000050886}.
FT DOMAIN 29..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 494 AA; 51231 MW; F1B75ACCD6AB162C CRC64;
MSTVATATSL EEILARLAPA HGVHIGGAWL RGDLGTYDVD DPADKAVLAA VGNAGADQAT
AAVDAAAAAA AGWAATPPRR RSEILHRAFE LMRRDADELA TLICAENGKS VADARAEVAY
AGEFFRWFAE EAVRIDGSFG SAPAGGVRSV VTRRPVGIAA LVTPWNFPAA MATRKIAPAL
AAGCTVVLKP AAETPLTAFA VARLLAEAGV PAGVVNVVPT TEPDDVVGTW LADPRVRKIS
FTGSTGVGRH LLRQAADRVL NASMELGGNA PFVVTEDADV VAAVDGAMVA KFRGGGQACT
AANRLYVHVA VAEEFTALLA QRVSALVVGR GAEPGTEIGP LINARAVDRV NGLLDDALAG
GARVVARAEV PDGLSGYFLA PTVVADVAPD ARLVQEEIFA PVAPIVTWDD EDTLVELVND
SEMGLAAYVF AGDLKRALQL AERIDAGMVG INRGLVSDPS APFGGLKQSG LGREGAHEGL
EEYQETQYFS VDWS
//
