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Database: UniProt
Entry: A0A0Q3WXV2_9BACI
LinkDB: A0A0Q3WXV2_9BACI
Original site: A0A0Q3WXV2_9BACI 
ID   A0A0Q3WXV2_9BACI        Unreviewed;       474 AA.
AC   A0A0Q3WXV2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KQL53900.1};
DE            EC=1.2.1.16 {ECO:0000313|EMBL:KQL53900.1};
GN   Name=gabD {ECO:0000313|EMBL:KQL53900.1};
GN   ORFNames=AN964_10580 {ECO:0000313|EMBL:KQL53900.1};
OS   Heyndrickxia shackletonii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL53900.1, ECO:0000313|Proteomes:UP000051888};
RN   [1] {ECO:0000313|EMBL:KQL53900.1, ECO:0000313|Proteomes:UP000051888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL53900.1,
RC   ECO:0000313|Proteomes:UP000051888};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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:KQL53900.1}.
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DR   EMBL; LJJC01000004; KQL53900.1; -; Genomic_DNA.
DR   RefSeq; WP_055739640.1; NZ_LJJC01000004.1.
DR   AlphaFoldDB; A0A0Q3WXV2; -.
DR   STRING; 157838.AN964_10580; -.
DR   PATRIC; fig|157838.3.peg.2328; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000051888; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KQL53900.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051888}.
FT   DOMAIN          12..470
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   474 AA;  51713 MW;  21E7278CA51336F7 CRC64;
     MYIEKMYING EWLTSADTIE VFNPATKEKI GVVPNGGQRE AELAVSAAFS ALPSWSKRTA
     AERSKYLMKW SQLIDENLNT LAEIMTNEQG KPLHEAKGEI TYANDYIVWY AEEAKRIYGE
     TIPASHPNKR IFVQKQPIGV VAAITPWNFP AAMITRKIAP AIAAGCTTVL KPSEETPFTA
     LKLVELAEQA GIPKGVINII TGDAPTIANV WQSDRRVRKL TFTGSTEVGK ILMRGAAETV
     KKVSLELGGH APFIVTANAD IEKAVDGAIA SKFRNAGQTC VCTNRIYVDK SIVKEFTQKF
     TEKVSCLKVG NGLDEGVVIG PLINQEAMDK VNNHIEDAIQ KGGTVYVGGN PLKELDGYFF
     EPTVITDATD DMFCMYEETF GPLAPITTFD TIEEVVERAN NTPYGLAAYV FTENIKEAIQ
     IAESLEYGII GLNDGTPSAA QAPFGGFKES GLGREGSHFG IEDYLEIKYI SLGL
//
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