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Protein

Alanine dehydrogenase

Gene

ald

Organism
Phormidium lapideum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151PyruvateCombined sources
Binding sitei74 – 741PyruvateCombined sources
Sitei74 – 741Important for catalytic activityCombined sources
Sitei95 – 951Important for catalytic activityCombined sources
Sitei117 – 1171Important for catalytic activityCombined sources
Sitei269 – 2691Important for catalytic activityCombined sources

GO - Molecular functioni

  1. alanine dehydrogenase activity Source: UniProtKB-EC
  2. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. L-alanine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

NADUniRule annotationCombined sources, Nucleotide-bindingCombined sources, PyruvateCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12816.
UniPathwayiUPA00527; UER00585.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine dehydrogenaseUniRule annotation (EC:1.4.1.1UniRule annotation)
Gene namesi
Name:aldImported
OrganismiPhormidium lapideumImported
Taxonomic identifieri32060 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesPhormidium

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJBX-ray2.10A1-361[»]
1PJCX-ray2.00A1-361[»]
1SAYX-ray2.10A1-361[»]
ProteinModelPortaliO52942.
SMRiO52942. Positions 1-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52942.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 953Pyruvate bindingCombined sources

Sequence similaritiesi

Belongs to the AlaDH/PNT family.UniRule annotation

Family and domain databases

InterProiIPR008141. Ala_DH.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000183. Alanine_dh. 1 hit.
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00518. alaDH. 1 hit.
PROSITEiPS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O52942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIGVPKEIK NQEFRVGLSP SSVRTLVEAG HTVFIETQAG IGAGFADQDY
60 70 80 90 100
VQAGAQVVPS AKDAWSREMV VKVKEPLPAE YDLMQKDQLL FTYLHLAAAR
110 120 130 140 150
ELTEQLMRVG LTAIAYETVE LPNRSLPLLT PMSIIAGRLS VQFGARFLER
160 170 180 190 200
QQGGRGVLLG GVPGVKPGKV VILGGGVVGT EAAKMAVGLG AQVQIFDINV
210 220 230 240 250
ERLSYLETLF GSRVELLYSN SAEIETAVAE ADLLIGAVLV PGRRAPILVP
260 270 280 290 300
ASLVEQMRTG SVIVDVAVDQ GGCVETLHPT SHTQPTYEVF GVVHYGVPNM
310 320 330 340 350
PGAVPWTATQ ALNNSTLPYV VKLANQGLKA LETDDALAKG LNVQAHRLVH
360
PAVQQVFPDL A
Length:361
Mass (Da):38,557
Last modified:June 1, 1998 - v1
Checksum:i57CA14BB85DB4D08
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37807 Genomic DNA. Translation: BAA24455.1.
PIRiPX0078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37807 Genomic DNA. Translation: BAA24455.1.
PIRiPX0078.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJBX-ray2.10A1-361[»]
1PJCX-ray2.00A1-361[»]
1SAYX-ray2.10A1-361[»]
ProteinModelPortaliO52942.
SMRiO52942. Positions 1-361.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00527; UER00585.
BioCyciMetaCyc:MONOMER-12816.

Miscellaneous databases

EvolutionaryTraceiO52942.

Family and domain databases

InterProiIPR008141. Ala_DH.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000183. Alanine_dh. 1 hit.
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00518. alaDH. 1 hit.
PROSITEiPS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum."
    Sawa Y., Tani M., Murata K., Shibata H., Ochiai H.
    J. Biochem. 116:995-1000(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Alanine Dehydrogenase from a Cyanobacterium, Phormidium lapideum: Cloning, Sequencing, Expression, and Sequence Comparisons to Amino Acid Dehydrogenases."
    Sawa Y., Noshiro Y., Midorikawa Y., Sasai R., Murata K., Ashida H., Shibata H., Ochiai H.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase."
    Baker P.J., Sawa Y., Shibata H., Sedelnikova S.E., Rice D.W.
    Nat. Struct. Biol. 5:561-567(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD AND PYRUVATE, ACTIVE SITE.

Entry informationi

Entry nameiO52942_PHOLP
AccessioniPrimary (citable) accession number: O52942
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.