NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 10208 / NRS 966 / NCIB 11935 / 1911;
DOI=10.1021/bi00456a025; PubMed=2340274 [NCBI, ExPASy, EBI, Israel, Japan]
Kuroda S., Tanizawa K., Sakamoto Y., Tanaka H., Soda K.;
"Alanine dehydrogenases from two Bacillus species with distinct thermostabilities: molecular cloning, DNA and protein sequence determination, and structural comparison with other NAD(P)(+)-dependent dehydrogenases.";
Biochemistry 29:1009-1015(1990).

Comments

FUNCTION: This enzyme is a key factor in the assimilation of L-alanine as an energy source through the tricarboxylic acid cycle during sporulation.
CATALYTIC ACTIVITY: L-alanine + H₂O + NAD⁺ = pyruvate + NH₃ + NADH.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Loses about 50% of its initial activity when heated at 65 degrees Celsius for 5 min;
PATHWAY: Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1 .
SUBUNIT: Homohexamer.
SUBCELLULAR LOCATION: Cytoplasm.
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

M33298; AAA22210.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34261; A34261.

3D structure databases

HSSP

O52942; 1SAY. [HSSP ENTRY / PDB]

ModBase

P17556.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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

P17556.

Other

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 372`	`372`	`Alanine dehydrogenase.`	`PRO_0000198990`
`NP_BIND`	`170 200`	`31`	`NAD (By similarity).`
`ACT_SITE`	`96 96`		`Potential.`

Sequence information

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

Molecular weight: 39460 Da [This is the MW of the unprocessed precursor]

CRC64: 5E6FD5E4D93AA98B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIGIPKEIK NNENRVAMTP AGVVSLTHAG HERLAIETGG GIGSSFTDAE YVAAGAAYRC 

        70         80         90        100        110        120 
IGKEAWAQEM ILKVKEPVAS EYDYFYEGQI LFTYLHLAPR AELTQALIDK KVVGIAYETV 

       130        140        150        160        170        180 
QLANGSLPLL TPMSEVAGKM ATQIGAQYLE KNHGGKGILL GGVSGVHARK VTVIGGGIAG 

       190        200        210        220        230        240 
TNAAKIAVGM GADVTVIDLS PERLRQLEDM FGRDVQTLMS NPYNIAESVK HSDLVVGAVL 

       250        260        270        280        290        300 
IPGAKAPKLV SEEMIQSMQP GSVVVDIAID QGGIFATSDR VTTHDDPTYV KHGVVHYAVA 

       310        320        330        340        350        360 
NMPGAVPRTS TIALTNNTIP YALQIANKGY KQACIDNPAL KKGVNALEGH ITYKAVAEAQ 

       370 
GLPYVNVDEL IQ

P17556 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