Q0K845 (SAUS_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfoacetaldehyde dehydrogenase (acylating)
EC=1.2.1.81

Gene names

Name:	sauS
Ordered Locus Names:	H16_A2747

Organism

Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus necator

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of sulfoacetyl-CoA and NADPH to sulfoacetaldehyde, CoA and NADP+. Specific for NADP+ and sulfoacetaldehyde. Ref.2
Catalytic activity	2-sulfoacetaldehyde + CoA + NADP+ = sulfoacetyl-CoA + NADPH. Ref.2
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm Ref.2.
Induction	Induced by sulfoacetate. Ref.2
Disruption phenotype	Mutants do not grow with sulfoacetate, but can use acetate, taurine, isethionate and sulfoacetaldehyde. Ref.2
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=64 µM for NADP+ Ref.2 KM=102 µM for CoA KM=330 µM for sulfoacetaldehyde pH dependence: Optimum pH is 9.0.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 493	492	Sulfoacetaldehyde dehydrogenase (acylating)		PRO_0000418824
Sites
	Active site	273	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0K845 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 05578252ACF80005	FASTA	493	51,647
	10 20 30 40 50 60 MSVQILHRRQ SNNSDLPLPT ASLPVQPAQA AAEAVAAVVA RARQAQREFA RADQATVDTA 70 80 90 100 110 120 VAAAAWAIME PARNRQLAER AVADTGLGNV DDKIRKNHRK TLGLLRDLHG RRTVGVIAQD 130 140 150 160 170 180 AAAGITEIAR PVGVVAAITP STNPAATPAN KIINALKCGN SVILAPSPKG QDTCALLLSF 190 200 210 220 230 240 IHAEFARAGL PADLVQMLPA PVSKTATAEL MRQADLVVAT GSQANVRMAY TCGTPAFGVG 250 260 270 280 290 300 AGNVASIIDA SATLDDAAAK VARSKTFDNA TSCSSENSLV VVDAVYTPML DALAAVGGVL 310 320 330 340 350 360 LTASEKARLQ ALMWRDAKLA GSFTGQSATR IAELAGLERV RALQPAMLLV EETGVGSDYP 370 380 390 400 410 420 FSGEKLSPVL TLYRATDFAA AVERVASLYA YMGAGHSVSL HSSNPRHALQ LGQELPVARV 430 440 450 460 470 480 IVNQAHCFAT GGNFDNGLPF SLSMGCGTWG GNNFSDNLGW RQYLNITRIA VPIAEHVPDE 490 ADLLGDYFAR VGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
[2]	"Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and sulfoacetaldehyde in Cupriavidus necator H16." Weinitschke S., Hollemeyer K., Kusian B., Bowien B., Smits T.H., Cook A.M. J. Biol. Chem. 285:35249-35254(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-7, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, GENE NAME. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM260479 Genomic DNA. Translation: CAJ93826.1.
RefSeq	YP_727194.1. NC_008313.1.
3D structure databases
ProteinModelPortal	Q0K845.
ModBase	Search...
Protein-protein interaction databases
STRING	381666.H16_A2747.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ93826; CAJ93826; H16_A2747.
GeneID	4250430.
KEGG	reh:H16_A2747.
PATRIC	35235023. VBIRalEut6770_3143.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HOG000289181.
KO	K15515.
OMA	SLSMGCG.
ProtClustDB	CLSK939330.
Enzyme and pathway databases
BioCyc	CNEC381666:GJUJ-2712-MONOMER. MetaCyc:MONOMER-15852.
Family and domain databases
Gene3D	3.40.309.10. 2 hits. 3.40.605.10. 1 hit.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view]
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SAUS_CUPNH

Accession

Primary (citable) accession number: Q0K845

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program