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Database: UniProt
Entry: A0A0N8VSD4_9PSED
LinkDB: A0A0N8VSD4_9PSED
Original site: A0A0N8VSD4_9PSED 
ID   A0A0N8VSD4_9PSED        Unreviewed;       480 AA.
AC   A0A0N8VSD4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KQB53012.1};
DE            EC=1.2.1.16 {ECO:0000313|EMBL:KQB53012.1};
GN   Name=gabD {ECO:0000313|EMBL:KQB53012.1};
GN   ORFNames=AQS70_12070 {ECO:0000313|EMBL:KQB53012.1};
OS   Pseudomonas endophytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB53012.1, ECO:0000313|Proteomes:UP000050342};
RN   [1] {ECO:0000313|EMBL:KQB53012.1, ECO:0000313|Proteomes:UP000050342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSTT44 {ECO:0000313|EMBL:KQB53012.1,
RC   ECO:0000313|Proteomes:UP000050342};
RA   Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT   "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT   isolated from raw cows milk.";
RL   Submitted (OCT-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:KQB53012.1}.
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DR   EMBL; LLWH01000178; KQB53012.1; -; Genomic_DNA.
DR   RefSeq; WP_055103521.1; NZ_LLWH01000178.1.
DR   AlphaFoldDB; A0A0N8VSD4; -.
DR   STRING; 1563157.AQS70_12070; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000050342; Unassembled WGS sequence.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; 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; 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   InterPro; IPR010102; Succ_semiAld_DH.
DR   NCBIfam; TIGR01780; SSADH; 1.
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; 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          19..475
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   480 AA;  51372 MW;  154B11AA8FC0CB5A CRC64;
     MQLKDAQLFR QQAYVDGAWV DADGGQTIKV NNPATGEVIG TVPKMGAVET RRAIEAADKA
     LPAWRALTAK ERAGKLRRWF ELLIENQDDL GRLMTLEQGK PLAEAKGEIA YAASFIEWFA
     EEAKRVYGDV IPGHQPDKRL IVIKQPIGVT AAITPWNFPA AMITRKAGPA LAAGCTMVIK
     PASQTPFSAL ALVELAHRAG IPKGVLSVVT GSAGDIGGEL TSNPIVRKLS FTGSTEIGRQ
     LMAECAKDIK KVSLELGGNA PFIVFDDADL DKAVEGAIIS KYRNNGQTCV CANRLYIQDG
     VYDAFAEKLK AAVAKLKIGN GLEEGTTTGP LIDDKAVAKV KEHIADAVSK GATVLAGGNS
     LEGSFFEPTI LVNVPKNAAV AKEETFGPLA PLFRFKDEAE VIELANDTEF GLASYFYARD
     MSRVFRVAEA LEYGMVGVNT GLISNEVAPF GGIKASGLGR EGSKYGIEDY LEIKYLCLSI
//
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