P99120 (BUTA_STAAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diacetyl reductase [(S)-acetoin forming]
EC=1.1.1.304

Alternative name(s):
Acetoin(diacetyl) reductase
Short name=AR
Meso-2,3-butanediol dehydrogenase

Gene names

Name:	butA
Ordered Locus Names:	SA0122

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH By similarity.
Catalytic activity	(S)-acetoin + NAD+ = diacetyl + NADH.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetoin catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	diacetyl reductase ((S)-acetoin forming) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	Diacetyl reductase [(S)-acetoin forming]		PRO_0000054541
Regions
	Nucleotide binding	8 – 32	25	NAD By similarity
Sites
	Active site	154	1	Proton acceptor By similarity
	Active site	158	1	By similarity
	Binding site	141	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99120 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 114AFD0DC5D780CF	FASTA	258	27,216
	10 20 30 40 50 60 MTNNKVALVT GGAQGIGFKI AERLVEDGFK VAVVDFNEEG AKAAALKLSS DGTKAIAIKA 70 80 90 100 110 120 DVSNRDDVFN AVRQTAAQFG DFHVMVNNAG LGPTTPIDTI TEEQFKTVYG VNVAGVLWGI 130 140 150 160 170 180 QAAHEQFKKF NHGGKIINAT SQAGVEGNPG LSLYCSTKFA VRGLTQVAAQ DLASEGITVN 190 200 210 220 230 240 AFAPGIVQTP MMESIAVATA EEAGKPEAWG WEQFTSQIAL GRVSQPEDVS NVVSFLAGKD 250 SDYITGQTII VDGGMRFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB41341.1.
PIR	B89773.
RefSeq	NP_373363.1. NC_002745.2.
3D structure databases
ProteinModelPortal	P99120.
SMR	P99120. Positions 4-257.
ModBase	Search...
Protein-protein interaction databases
STRING	P99120.
2D gel databases
SWISS-2DPAGE	P99120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000000740; EBSTAP00000000740; EBSTAG00000000740.
GeneID	1122896.
GenomeReviews	Gene locus SA0122 in contig BA000018_GR.
KEGG	sau:SA0122.
PATRIC	19572273. VBIStaAur116463_0126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1028.
GeneTree	EBGT00050000023864.
HOGENOM	HBG750976.
OMA	VAACVAY.
ProtClustDB	PRK08643.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0122-MONOMER.
Family and domain databases
InterPro	IPR014007. 23BDH. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K03366.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
TIGRFAMs	TIGR02415. 23BDH. 1 hit.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BUTA_STAAN

Accession

Primary (citable) accession number: P99120
Secondary accession number(s): Q99X89

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program