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Database: UniProt
Entry: A0A258NTM8_9BURK
LinkDB: A0A258NTM8_9BURK
Original site: A0A258NTM8_9BURK 
ID   A0A258NTM8_9BURK        Unreviewed;       492 AA.
AC   A0A258NTM8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase (NADP(+)) {ECO:0000313|EMBL:OYY33665.1};
GN   Name=gabD {ECO:0000313|EMBL:OYY33665.1};
GN   ORFNames=B7Y60_18685 {ECO:0000313|EMBL:OYY33665.1};
OS   Polaromonas sp. 35-63-35.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY33665.1, ECO:0000313|Proteomes:UP000216365};
RN   [1] {ECO:0000313|EMBL:OYY33665.1, ECO:0000313|Proteomes:UP000216365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35-63-35 {ECO:0000313|EMBL:OYY33665.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYY33665.1}.
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DR   EMBL; NCFQ01000016; OYY33665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258NTM8; -.
DR   Proteomes; UP000216365; 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          27..484
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   492 AA;  52866 MW;  8DDA08520B4C6BF3 CRC64;
     MDMKTSPISL LKDPSLFKTD ALINGQWVKG SSRFDVNDPS TGLKLADVAN LGAKEAEAAI
     AAANAAWPAW RSKTGKERHA ILLKWYQLLM ANVEDLGRIM TAEQGKPFTE AKGEVTYGAS
     FVEWFAEEAK RVNGETLPQF DNNRRLMVLK QPIGVCAAIT PWNFPLAMIT RKVAPALAAG
     CPVVIKPAEL TPLTALAAAE LAVRAGVPAG VLNVLTADSD NSIAAGKVFC ASDVVRHISF
     TGSTEVGRIL MAQSAPSIKK LSLELGGNAP FIVFDDADID SAVDGAMASK YRNAGQTCVC
     ANRIYVQDGV YDKFVEKFAA KVKLLKVGNG FEEGVVQGPL IEDAAVEKVQ RHVDDAIARG
     GKLMAGGKKL KGQFFEPTVI SEATGDMLCA KEETFGPFAP VFRFKHEQEA IDAANNTEFG
     LASYFYSRDI GRIYRVAEAL EYGMVGINAG VIATEHVPFG GVKQSGLGRE GSSHGMEEYL
     EMKYLCLGDI LK
//
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