[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; Lancet 357:1225-1240(2001).
[2]	IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1016/j.mimet.2004.09.017; PubMed=15590099 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."; J. Microbiol. Methods 60:247-257(2005).
[3]	IDENTIFICATION BY MASS SPECTROMETRY. Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.; "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."; Submitted (OCT-2007) to UniProtKB.

Comments

FUNCTION: May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer (By similarity).
CATALYTIC ACTIVITY: L-alanine + H₂O + NAD⁺ = pyruvate + NH₃ + NADH.
PATHWAY: Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1 .
SIMILARITY: Belongs to the AlaDH/PNT family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000018; BAB42532.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G89921; G89921.

RefSeq

NP_374553.1; -.

3D structure databases

HSSP

O52942; 1SAY. [HSSP ENTRY / PDB]

ModBase

P99151.

Enzyme and pathway databases

BioCyc

SAUR158879:SA1272-MON; -.

2D gel databases

SWISS-2DPAGE

P99151; -.

Ontologies

GO:0000286;	Molecular function: alanine dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007698; Ala_DHase/PNT_C.
IPR008142; Ala_DHase/PNT_CS1.
IPR008143; Ala_DHase/PNT_CS2.
IPR007886; Ala_DHase/PNT_N.
IPR008141; Ala_DHase_PNT.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00518; alaDH; 1.

PROSITE

PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.

ProtoNet

P99151.

Genome annotation databases

GeneID

1124110; -.

GenomeReviews

BA000018_GR; SA1272.

KEGG

sau:SA1272; -.

Phylogenomic databases

HOGENOM

P99151; -.

Genome annotation databases

CMR

P99151; SA1272.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 372`	`372`	`Alanine dehydrogenase 1.`	`PRO_0000198997`
`NP_BIND`	`170 200`	`31`	`NAD (By similarity).`
`ACT_SITE`	`94 94`		`Potential.`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 40235 Da [This is the MW of the unprocessed precursor]

CRC64: CAF521B4A8C5D8EC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLVAVVKELK QGEGRVACTP ENVRKLTDAG HKVIVEKNAG IGSGFSNDMY EKEGAKIVTH 

        70         80         90        100        110        120 
EQAWEADLVI KVKEPHESEY QYFKKNQIIW GFLHLASSKE IVEKMQEVGV TAISGETIIK 

       130        140        150        160        170        180 
NGKAELLAPM SAIAGQRSAI MGAYYSEAQH GGQGTLVTGV HENVDIPGST YVIFGGGVAA 

       190        200        210        220        230        240 
TNAANVALGL NAKVIIIELN DDRIKYLEDM YAEKDVTVVK STPENLAEQI KKADVFISTI 

       250        260        270        280        290        300 
LIPGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP 

       310        320        330        340        350        360 
NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL STGVNIYQGQ VTNQGLASSH 

       370 
DLDYKEILNV IE

P99151 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools