Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P17556 (DHA_BACSH)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanine dehydrogenase
    EC=1.4.1.1
Gene names
Name: ald
OrganismBacillus sphaericus
Taxonomic identifier1421 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesPlanococcaceaeLysinibacillus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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.

Pathway

Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the AlaDH/PNT family.

biophysicochemical properties

Temperature dependence:

Loses about 50% of its initial activity when heated at 65 degrees Celsius for 5 min.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalanine dehydrogenase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Alanine dehydrogenase
PRO_0000198990

Regions

Nucleotide binding170 – 20031NAD By similarity

Sites

Active site961 Potential

Sequences

Sequence LengthMass (Da)Tools
P17556-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 5E6FD5E4D93AA98B

FASTA37239,460
        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 

« Hide

References

[1]"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."
Kuroda S., Tanizawa K., Sakamoto Y., Tanaka H., Soda K.
Biochemistry 29:1009-1015(1990) [PubMed: 2340274] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 10208 / NRS 966 / NCIB 11935 / 1911.

Cross-references

Sequence databases

M33298 Genomic DNA. Translation: AAA22210.1.
PIRA34261.

3D structure databases

HSSPHSSP built from PDB template 1SAY based on UniProtKB O52942.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.1.1. 327.

Family and domain databases

InterProIPR007698. Ala_DH/PNT_C.
IPR008142. Ala_DH/PNT_CS1.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. Ala_DH/PNT_N.
IPR008141. Ala_DH_PNT.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00518. alaDH. 1 hit.
PROSITEPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHA_BACSH
AccessionPrimary (citable) accession number: P17556
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents