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Database: UniProt
Entry: A0A0Q9S328_9MICO
LinkDB: A0A0Q9S328_9MICO
Original site: A0A0Q9S328_9MICO 
ID   A0A0Q9S328_9MICO        Unreviewed;       487 AA.
AC   A0A0Q9S328;
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:KRF22273.1};
GN   ORFNames=ASG91_18255 {ECO:0000313|EMBL:KRF22273.1};
OS   Phycicoccus sp. Soil802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF22273.1, ECO:0000313|Proteomes:UP000050906};
RN   [1] {ECO:0000313|EMBL:KRF22273.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF22273.1,
RC   ECO:0000313|Proteomes:UP000050906};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF22273.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF22273.1,
RC   ECO:0000313|Proteomes:UP000050906};
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:KRF22273.1}.
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DR   EMBL; LMSS01000007; KRF22273.1; -; Genomic_DNA.
DR   RefSeq; WP_056924058.1; NZ_LMSS01000007.1.
DR   AlphaFoldDB; A0A0Q9S328; -.
DR   Proteomes; UP000050906; 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}.
FT   DOMAIN          24..484
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   487 AA;  51060 MW;  3D106ACBAFFAEBDD CRC64;
     MTLSPAEQAL VAAVPTGLFI NGAWCEASDG ARVPVEDPST GLAFASVADA TVTDGGDALA
     AASAAQASWA ATAPRERGEL LLAAYELLTE RAEDFATLMT LEMGKPLAEA RGEVAYGAEF
     FRWFSEEAVR ISGRWMTAPN GATRLLTMKK PVGPTLMVTP WNFPLAMGTR KIGPAIAAGC
     TMVVKPATQT PLSMLALAAL LDEVGLPAGV LNVITTTRTA AVMEPLIRDP RARKLTFTGS
     TPVGRTLVEQ SATQLLRVSM ELGGNAPFIV FDDADLDAAV DGAMLAKMRN MGEACTAANR
     FLVQSGVADE FATRLTARME QLSIGRGTEA GVDVGPLIDA PAQAKVEELV DDAVLRGARV
     ACGGKPVGET GHFYAPTVLT DVPADARLLR EEIFGPVAAI ATFDTEDEAI SRANDTEYGL
     AAYVFSRDLS RVLRLAEQLE VGMVGVNQGI VSNPAAPFGG MKASGFGREG GLEGIEEYLE
     TTYVGIA
//
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