Reviewed, UniProtKB/Swiss-Prot P17557 (DHA_BACST)

Names and origin

Protein names

Recommended name:
    Alanine dehydrogenase
    EC=1.4.1.1

Gene names

Name:

ald

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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: Retains about 50% of its initial activity when heated at 85 degrees Celsius for 5 min at pH 7.2.

Ontologies

Keywords
Biological process	Sporulation
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alanine 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 372	372	Alanine dehydrogenase		PRO_0000198991
Regions
	Nucleotide binding	170 – 200	31	NAD By similarity
Sites
	Active site	96	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	P17557-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 99AE8E621ED1F23A	FASTA	372	39,695
	10 20 30 40 50 60 MKIGIPKEIK NNENRVAITP AGVMTLVKAG HEVYVETEGG AGSGFSDSEY EKAGAADRCR 70 80 90 100 110 120 TWRDAWTAEM VLKVKEPLAR EFRYFRPGLI LFTYLHLAAA ERVTKAVVEQ KVVGIAYETV 130 140 150 160 170 180 QLANGSLPLL TPMSEVAGRM SVQVGAQFLE KPHGGKGILL GGVPGVRRGK VTIIGGGTAG 190 200 210 220 230 240 TNAAKIGVGL GADVTILDIN AERLRELDDL FGDHVTTLMS NSYHIAECVR ESDLVVGAVL 250 260 270 280 290 300 IPGAKAKLVT EEMVRSMTPG SVLVDIAIDQ GGIFETTDRV TTHDDPTYVK HGVVHYAVAN 310 320 330 340 350 360 MPGAVPRTST FALTNVTIPY ALQIANKGYR AGCLDNPALL KGINTLDGHI VYEAVAAAHN 370 MPYTDVHSLL HG

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 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33299 Genomic DNA. Translation: AAA22211.1.
PIR	B34261.
3D structure databases
HSSP	HSSP built from PDB template 1SAY based on UniProtKB O52942.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.4.1.1. 266715.
Family and domain databases
InterPro	IPR007698. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00518. alaDH. 1 hit.
PROSITE	PS00836. ALADH_PNT_1. 1 hit. PS00837. ALADH_PNT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHA_BACST

Accession

Primary (citable) accession number: P17557

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)