ID   SAUS_CUPNH              Reviewed;         493 AA.
AC   Q0K845;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Sulfoacetaldehyde dehydrogenase (acylating);
DE            EC=1.2.1.81;
GN   Name=sauS; OrderedLocusNames=H16_A2747;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-7, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE,
RP   AND GENE NAME.
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=20693281; DOI=10.1074/jbc.m110.127043;
RA   Weinitschke S., Hollemeyer K., Kusian B., Bowien B., Smits T.H., Cook A.M.;
RT   "Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and
RT   sulfoacetaldehyde in Cupriavidus necator H16.";
RL   J. Biol. Chem. 285:35249-35254(2010).
CC   -!- FUNCTION: Catalyzes the conversion of sulfoacetyl-CoA and NADPH to
CC       sulfoacetaldehyde, CoA and NADP(+). Specific for NADP(+) and
CC       sulfoacetaldehyde. {ECO:0000269|PubMed:20693281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + NADP(+) + sulfoacetaldehyde = H(+) + NADPH +
CC         sulfoacetyl-CoA; Xref=Rhea:RHEA:29595, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58246,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:61994; EC=1.2.1.81;
CC         Evidence={ECO:0000269|PubMed:20693281};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=64 uM for NADP(+) {ECO:0000269|PubMed:20693281};
CC         KM=102 uM for CoA {ECO:0000269|PubMed:20693281};
CC         KM=330 uM for sulfoacetaldehyde {ECO:0000269|PubMed:20693281};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:20693281};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20693281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20693281}.
CC   -!- INDUCTION: Induced by sulfoacetate. {ECO:0000269|PubMed:20693281}.
CC   -!- DISRUPTION PHENOTYPE: Mutants do not grow with sulfoacetate, but can
CC       use acetate, taurine, isethionate and sulfoacetaldehyde.
CC       {ECO:0000269|PubMed:20693281}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM260479; CAJ93826.1; -; Genomic_DNA.
DR   RefSeq; WP_011615809.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0K845; -.
DR   SMR; Q0K845; -.
DR   STRING; 381666.H16_A2747; -.
DR   PRIDE; Q0K845; -.
DR   EnsemblBacteria; CAJ93826; CAJ93826; H16_A2747.
DR   GeneID; 57644871; -.
DR   KEGG; reh:H16_A2747; -.
DR   PATRIC; fig|381666.6.peg.3143; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_028794_3_0_4; -.
DR   OMA; IVNQAHC; -.
DR   OrthoDB; 384611at2; -.
DR   BioCyc; MetaCyc:MON-15852; -.
DR   BRENDA; 1.2.1.81; 231.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:20693281"
FT   CHAIN           2..493
FT                   /note="Sulfoacetaldehyde dehydrogenase (acylating)"
FT                   /id="PRO_0000418824"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        273
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  51647 MW;  05578252ACF80005 CRC64;
     MSVQILHRRQ SNNSDLPLPT ASLPVQPAQA AAEAVAAVVA RARQAQREFA RADQATVDTA
     VAAAAWAIME PARNRQLAER AVADTGLGNV DDKIRKNHRK TLGLLRDLHG RRTVGVIAQD
     AAAGITEIAR PVGVVAAITP STNPAATPAN KIINALKCGN SVILAPSPKG QDTCALLLSF
     IHAEFARAGL PADLVQMLPA PVSKTATAEL MRQADLVVAT GSQANVRMAY TCGTPAFGVG
     AGNVASIIDA SATLDDAAAK VARSKTFDNA TSCSSENSLV VVDAVYTPML DALAAVGGVL
     LTASEKARLQ ALMWRDAKLA GSFTGQSATR IAELAGLERV RALQPAMLLV EETGVGSDYP
     FSGEKLSPVL TLYRATDFAA AVERVASLYA YMGAGHSVSL HSSNPRHALQ LGQELPVARV
     IVNQAHCFAT GGNFDNGLPF SLSMGCGTWG GNNFSDNLGW RQYLNITRIA VPIAEHVPDE
     ADLLGDYFAR VGK