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
//