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Database: UniProt
Entry: L0WDC5_9GAMM
LinkDB: L0WDC5_9GAMM
Original site: L0WDC5_9GAMM 
ID   L0WDC5_9GAMM            Unreviewed;       485 AA.
AC   L0WDC5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:EKF74137.1};
GN   ORFNames=A11A3_09972 {ECO:0000313|EMBL:EKF74137.1};
OS   Alcanivorax hongdengensis A-11-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF74137.1, ECO:0000313|Proteomes:UP000010164};
RN   [1] {ECO:0000313|EMBL:EKF74137.1, ECO:0000313|Proteomes:UP000010164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-11-3 {ECO:0000313|EMBL:EKF74137.1,
RC   ECO:0000313|Proteomes:UP000010164};
RX   PubMed=23209226; DOI=10.1128/JB.01849-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT   hongdengensis Type Strain A-11-3.";
RL   J. Bacteriol. 194:6972-6972(2012).
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:EKF74137.1}.
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DR   EMBL; AMRJ01000014; EKF74137.1; -; Genomic_DNA.
DR   RefSeq; WP_008929172.1; NZ_AMRJ01000014.1.
DR   AlphaFoldDB; L0WDC5; -.
DR   STRING; 1177179.A11A3_09972; -.
DR   PATRIC; fig|1177179.3.peg.1984; -.
DR   eggNOG; COG1012; Bacteria.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000010164; Unassembled WGS sequence.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
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          22..480
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   485 AA;  51409 MW;  2FB32651A6FC4B72 CRC64;
     MSAPSLSDSR LFRQQCYIDG QWCDADDGAT VDVDNPATEQ TLGTVPRMGA GETERAINAA
     NQALPAWRDK TAGERADILM AWFDLMMANQ DDLGRLMTLE QGKPLAEAKG EIAYAASFLK
     WFAEEARRAY GDTIPAPKPN QRIVVIKQPI GVCAAITPWN FPSSMITRKA GAALAAGCTM
     VVKPATATPY SALALAELAE RAGVPKGVFS VLTGSASAIA GALTDSPVVR KLSFTGSTEV
     GSTLMAQCAK HIQKVSLELG GNAPFIVFDD ANLDKAVDGA MASKFRNTGQ TCVCVNRFLV
     QDSVHDAFVE KLKTAIEAMK VGDGLEDGVT QAALINRGAA DKVMEHIEDA LGKGAKVITG
     GQRHEKGGSF VQPTLITGVS PDAQLCQEET FGPLAAVIPF SSEEEAIRIA NDTPYGLAAY
     FYSDNIHRCW RVAEALESGM VGVNEGLISN AAAPFGGVKE SGLGREGSHQ GMDEYLETKY
     LCMGS
//
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