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Database: UniProt
Entry: F2IVP2_POLGS
LinkDB: F2IVP2_POLGS
Original site: F2IVP2_POLGS 
ID   F2IVP2_POLGS            Unreviewed;       483 AA.
AC   F2IVP2;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase [NADP+] (SSDH) {ECO:0000313|EMBL:ADZ69149.1};
GN   Name=gabD1 {ECO:0000313|EMBL:ADZ69149.1};
GN   OrderedLocusNames=SL003B_0719 {ECO:0000313|EMBL:ADZ69149.1};
OS   Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Polymorphum.
OX   NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ69149.1, ECO:0000313|Proteomes:UP000008130};
RN   [1] {ECO:0000313|EMBL:ADZ69149.1, ECO:0000313|Proteomes:UP000008130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC   {ECO:0000313|Proteomes:UP000008130};
RX   PubMed=21478361; DOI=10.1128/JB.00333-11;
RA   Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT   "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT   degrading bacterium from oil-polluted saline soil.";
RL   J. Bacteriol. 193:2894-2895(2011).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP002568; ADZ69149.1; -; Genomic_DNA.
DR   RefSeq; WP_013651469.1; NC_015259.1.
DR   AlphaFoldDB; F2IVP2; -.
DR   STRING; 991905.SL003B_0719; -.
DR   KEGG; pgv:SL003B_0719; -.
DR   PATRIC; fig|991905.3.peg.729; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_1_5; -.
DR   OMA; EMKYLCQ; -.
DR   OrthoDB; 9802947at2; -.
DR   Proteomes; UP000008130; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008130}.
FT   DOMAIN          24..474
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   483 AA;  50951 MW;  D5855A41EC424ADC CRC64;
     MRSLTDPTLL KSQCYIDGCF VGEGRVDVTD PATGRVLAKV PDMGADQAVQ AVEVAAAAFK
     SWAALTARER STVLRAWFDL IMANRADLAA ILTSEQGKPY PEALGEIDYA ASFVEFYAEE
     AKRVLGEILP SHTTDARLLV LRQPIGVVAA ITPWNFPAAM ITRKIAPALA AGCTVVVKPA
     PETPLTALAL AELAHRAGFP KGTVNVLTGD AVAIGGVLTS HPKVRFVGFT GSTAVGKLLM
     AQAATTVKKV ALELGGNAPF IVFDDADLDA AVEGAIASKY RNMGQTCVCS NRFYVHDAVY
     DAFVDKLAAR VATLKVGNGF EEGVVQGPLI NERAVSKVER HISDALGKGA RVVAGGKRHT
     LGHTFFEPTV IADAAEGMQI AAEETFGPVA PVFRFHAEAE AIAAANNTES GLAAYFYARD
     VGRIFRVLEA LEYGMVGVNS GRISTELAPF GGIKESGNSR EGSHHGIAEF TELKYACIGG
     LTA
//
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