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Protein

Alanine dehydrogenase

Gene

ald

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible reductive amination of pyruvate to L-alanine. However, since the physiological environment of M.tuberculosis has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-alanine. May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.1 Publication

Miscellaneous

L-alanine dehydrogenase activity increases when the M.tuberculosis is shifted from aerobic to anaerobic growth conditions.1 Publication

Catalytic activityi

L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH.2 Publications

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by CuSO4 and ZnCl2.1 Publication

Kineticsi

  1. KM=98.2 µM for NADH (at pH 7.4 and at 37 degrees Celsius)1 Publication
  2. KM=0.31 mM for NAD (at pH 10.2 and at 37 degrees Celsius)1 Publication
  3. KM=0.76 mM for pyruvate (at pH 7.4 and at 25 degrees Celsius)1 Publication
  4. KM=1.45 mM for pyruvate (at pH 7.4 and at 37 degrees Celsius)1 Publication
  5. KM=13.8 mM for L-alanine (at pH 10.2 and at 37 degrees Celsius)1 Publication
  6. KM=15.6 mM for L-alanine (at pH 10.2 and at 25 degrees Celsius)1 Publication
  7. KM=35.4 mM for ammonium (at pH 7.4 and at 37 degrees Celsius)1 Publication
  1. Vmax=31.8 µmol/min/mg enzyme for reductive amination1 Publication
  2. Vmax=23.7 µmol/min/mg enzyme for oxidative deamination1 Publication

pH dependencei

Optimum pH is between 10 and 11 for the oxidative deamination and between 7 and 7.5 for the reductive amination.1 Publication

Temperature dependencei

Relatively stable, it loses only 25% of its total activity after 4 hours at 60 degrees Celsius. The enzyme is much more active at temperatures above 37 degrees Celsius, particularly in the reductive amination. The velocity almost doubles at temperatures between 60-65 degrees Celsius compared with 37 degrees Celsius. Above 65 degrees Celsius there is a sharp decrease in activity, due to thermal inactivation of the enzyme.2 Publications

Pathwayi: L-alanine degradation via dehydrogenase pathway

This protein is involved in step 1 of the subpathway that synthesizes NH(3) and pyruvate from L-alanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine dehydrogenase (LH57_15190), Alanine dehydrogenase (ald)
This subpathway is part of the pathway L-alanine degradation via dehydrogenase pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NH(3) and pyruvate from L-alanine, the pathway L-alanine degradation via dehydrogenase pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei15Substrate1 Publication1
Binding sitei75Substrate1 Publication1
Active sitei96Proton donor/acceptor1 Publication1
Binding sitei134NAD2 Publications1
Binding sitei198NAD2 Publications1
Binding sitei203NAD2 Publications1
Binding sitei220NAD2 Publications1
Active sitei270Proton donor/acceptor1 Publication1
Binding sitei279NAD2 Publications1
Metal bindingi323MagnesiumCombined sources1 Publication1
Metal bindingi327Magnesium; via tele nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi178 – 179NAD2 Publications2
Nucleotide bindingi239 – 240NAD2 Publications2
Nucleotide bindingi267 – 270NAD2 Publications4
Nucleotide bindingi298 – 301NAD2 Publications4

GO - Molecular functioni

GO - Biological processi

  • alanine catabolic process Source: MTBBASE
  • L-alanine catabolic process Source: UniProtKB-UniPathway
  • response to hypoxia Source: MTBBASE

Keywordsi

Molecular functionOxidoreductase
LigandMagnesium, Metal-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00527; UER00585.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine dehydrogenase (EC:1.4.1.12 Publications)
Alternative name(s):
40 kDa antigen
TB43
Gene namesi
Name:ald
Ordered Locus Names:Rv2780
ORF Names:MTV002.45
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2780.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96H → A: Completely inactive mutant. 1 Publication1
Mutagenesisi270D → A: Completely inactive mutant. 1 Publication1
Mutagenesisi270D → N: Completely inactive mutant. The bifurcated hydrogen bond between D-270 and the ribose of NAD is replaced by a single hydrogen bond. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001989941 – 371Alanine dehydrogenaseAdd BLAST371

Proteomic databases

PaxDbiP9WQB1.

Expressioni

Inductioni

Upon nutrient starvation.1 Publication

Interactioni

Subunit structurei

Homohexamer. Trimer of dimers.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv2780.

Structurei

Secondary structure

1371
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi20 – 28Combined sources9
Beta strandi32 – 36Combined sources5
Turni37 – 40Combined sources4
Helixi41 – 43Combined sources3
Helixi47 – 53Combined sources7
Beta strandi56 – 59Combined sources4
Helixi61 – 67Combined sources7
Beta strandi69 – 72Combined sources4
Helixi79 – 84Combined sources6
Beta strandi90 – 93Combined sources4
Helixi97 – 99Combined sources3
Helixi101 – 110Combined sources10
Beta strandi113 – 116Combined sources4
Helixi117 – 119Combined sources3
Turni128 – 130Combined sources3
Helixi131 – 148Combined sources18
Helixi151 – 153Combined sources3
Beta strandi170 – 174Combined sources5
Helixi178 – 189Combined sources12
Beta strandi193 – 199Combined sources7
Helixi201 – 210Combined sources10
Turni211 – 213Combined sources3
Beta strandi214 – 219Combined sources6
Helixi222 – 231Combined sources10
Beta strandi233 – 237Combined sources5
Beta strandi242 – 244Combined sources3
Helixi252 – 255Combined sources4
Beta strandi263 – 266Combined sources4
Helixi267 – 270Combined sources4
Beta strandi283 – 285Combined sources3
Beta strandi287 – 290Combined sources4
Beta strandi293 – 296Combined sources4
Helixi301 – 304Combined sources4
Helixi306 – 335Combined sources30
Helixi337 – 340Combined sources4
Beta strandi343 – 346Combined sources4
Helixi353 – 359Combined sources7
Beta strandi360 – 362Combined sources3
Helixi367 – 370Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VHVX-ray2.80A/B1-371[»]
2VHWX-ray2.00A/B/C/D/E/F1-371[»]
2VHXX-ray2.00A/B/C/D/E/F1-371[»]
2VHYX-ray2.30A/B1-371[»]
2VHZX-ray2.04A/B1-371[»]
2VOEX-ray2.60A/B/C/D/E/F1-371[»]
2VOJX-ray2.60A/C/E1-371[»]
ProteinModelPortaliP9WQB1.
SMRiP9WQB1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AlaDH/PNT family.Curated

Phylogenomic databases

eggNOGiENOG4105DCF. Bacteria.
COG0686. LUCA.
KOiK00259.
OMAiCFETSKA.
PhylomeDBiP9WQB1.

Family and domain databases

CDDicd05305. L-AlaDH. 1 hit.
InterProiView protein in InterPro
IPR008141. Ala_DH.
IPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR036291. NAD(P)-bd_dom_sf.
PANTHERiPTHR42795. PTHR42795. 1 hit.
PfamiView protein in Pfam
PF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PIRSFiPIRSF000183. Alanine_dh. 1 hit.
SMARTiView protein in SMART
SM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00518. alaDH. 1 hit.
PROSITEiView protein in PROSITE
PS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WQB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVGIPTETK NNEFRVAITP AGVAELTRRG HEVLIQAGAG EGSAITDADF
60 70 80 90 100
KAAGAQLVGT ADQVWADADL LLKVKEPIAA EYGRLRHGQI LFTFLHLAAS
110 120 130 140 150
RACTDALLDS GTTSIAYETV QTADGALPLL APMSEVAGRL AAQVGAYHLM
160 170 180 190 200
RTQGGRGVLM GGVPGVEPAD VVVIGAGTAG YNAARIANGM GATVTVLDIN
210 220 230 240 250
IDKLRQLDAE FCGRIHTRYS SAYELEGAVK RADLVIGAVL VPGAKAPKLV
260 270 280 290 300
SNSLVAHMKP GAVLVDIAID QGGCFEGSRP TTYDHPTFAV HDTLFYCVAN
310 320 330 340 350
MPASVPKTST YALTNATMPY VLELADHGWR AACRSNPALA KGLSTHEGAL
360 370
LSERVATDLG VPFTEPASVL A
Length:371
Mass (Da):38,713
Last modified:April 16, 2014 - v1
Checksum:i9DF7540524DC116A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13E → EFQ in CAA44791 (PubMed:1587598).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63069 Genomic DNA. Translation: CAA44791.1.
U92472 Genomic DNA. Translation: AAC38804.1.
AL123456 Genomic DNA. Translation: CCP45579.1.
PIRiC70883. A43830.
RefSeqiNP_217296.1. NC_000962.3.
WP_003899477.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45579; CCP45579; Rv2780.
GeneIDi888493.
KEGGimtu:Rv2780.

Similar proteinsi

Entry informationi

Entry nameiDHA_MYCTU
AccessioniPrimary (citable) accession number: P9WQB1
Secondary accession number(s): L0TC82, O33322, P30234
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 28, 2018
This is version 26 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome