[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 35801 / TMC 107 / Erdman; PubMed=1587598 [NCBI, ExPASy, EBI, Israel, Japan] Andersen A.B., Andersen P., Ljungqvist L.; "Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis."; Infect. Immun. 60:2317-2323(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 25618 / H37Rv; Singh M., Hutter B.; "Host-vector system for high level expression and purification of enzymatically active L-alanine dehydrogenase of M.tuberculosis in E.coli."; Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 25618 / H37Rv; DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan] Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."; Nature 393:537-544(1998).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CDC 1551 / Oshkosh; DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan] Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.; "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."; J. Bacteriol. 184:5479-5490(2002).
[5]	PROTEIN SEQUENCE OF 1-21. STRAIN=ATCC 25618 / H37Rv; PubMed=7822223 [NCBI, ExPASy, EBI, Israel, Japan] Deshpande R.G., Khan M.B., Bhat D.A., Navalkar R.G.; "Isolation of a 43 kDa protein from Mycobacterium tuberculosis H37Rv and its identification as a pyridine nucleotide transhydrogenase."; J. Appl. Bacteriol. 77:639-643(1994).

Comments

FUNCTION: May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.
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 .
SUBCELLULAR LOCATION: Secreted.
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

X63069; CAA44791.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U92472; AAC38804.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX842580; CAA15575.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK47169.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70883; A43830.

RefSeq

NP_217296.1; -.
NP_337355.1; -.

3D structure databases

PDB

2VHV; X-ray; 2.80 A; A/B=1-371.	[ExPASy / RCSB / EBI]
2VHW; X-ray; 2.00 A; A/B/C/D/E/F=1-371.	[ExPASy / RCSB / EBI]
2VHX; X-ray; 2.00 A; A/B/C/D/E/F=1-371.	[ExPASy / RCSB / EBI]
2VHY; X-ray; 2.30 A; A/B=1-371.	[ExPASy / RCSB / EBI]
2VHZ; X-ray; 2.04 A; A/B=1-371.	[ExPASy / RCSB / EBI]
2VOE; X-ray; 2.60 A; A/B/C/D/E/F=1-371.	[ExPASy / RCSB / EBI]
2VOJ; X-ray; 2.60 A; A/C/E=1-371.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2VHV; -.
2VHW; -.
2VHX; -.
2VHY; -.
2VHZ; -.
2VOE; -.
2VOJ; -.

ModBase

P30234.

Organism-specific databases

TubercuList

Rv2780; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (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.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00518; alaDH; 1.

PROSITE

PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.

Genome annotation databases

GeneID

888493; -.
925435; -.

GenomeReviews

AE000516_GR; MT2850.
AL123456_GR; Rv2780.

KEGG

mtc:MT2850; -.
mtu:Rv2780; -.

TIGR

MT2850; -.

Phylogenomic databases

HOGENOM

P30234; -.

Other

UniRef

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

Keywords

3D-structure; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Secreted.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 371`	`371`	`Alanine dehydrogenase.`	`PRO_0000198994`
`NP_BIND`	`170 200`	`31`	`NAD (By similarity).`
`ACT_SITE`	`96 96`		`Potential.`
`CONFLICT`	`13 13`		`E -> EFQ (in Ref. 1; CAA44791).`
`CONFLICT`	`123 123`		`A -> P (in Ref. 4; AAK47169).`
`STRAND`	`2 5`	`4`
`HELIX`	`20 28`	`9`
`STRAND`	`32 36`	`5`
`TURN`	`37 40`	`4`
`HELIX`	`41 43`	`3`
`HELIX`	`47 53`	`7`
`STRAND`	`56 59`	`4`
`HELIX`	`61 67`	`7`
`STRAND`	`69 72`	`4`
`HELIX`	`79 84`	`6`
`STRAND`	`90 93`	`4`
`HELIX`	`97 99`	`3`
`HELIX`	`101 110`	`10`
`STRAND`	`113 116`	`4`
`HELIX`	`117 119`	`3`
`TURN`	`128 130`	`3`
`HELIX`	`131 148`	`18`
`HELIX`	`151 153`	`3`
`STRAND`	`170 174`	`5`
`HELIX`	`178 189`	`12`
`STRAND`	`193 199`	`7`
`HELIX`	`201 210`	`10`
`TURN`	`211 213`	`3`
`STRAND`	`214 219`	`6`
`HELIX`	`222 231`	`10`
`STRAND`	`233 237`	`5`
`HELIX`	`252 255`	`4`
`STRAND`	`263 266`	`4`
`HELIX`	`267 270`	`4`
`STRAND`	`283 285`	`3`
`STRAND`	`287 290`	`4`
`STRAND`	`293 296`	`4`
`HELIX`	`301 304`	`4`
`HELIX`	`306 335`	`30`
`HELIX`	`337 340`	`4`
`STRAND`	`343 346`	`4`
`HELIX`	`353 359`	`7`
`HELIX`	`367 370`	`4`

Sequence information

Length: 371 AA [This is the length of the unprocessed precursor]

Molecular weight: 38713 Da [This is the MW of the unprocessed precursor]

CRC64: 9DF7540524DC116A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVGIPTETK NNEFRVAITP AGVAELTRRG HEVLIQAGAG EGSAITDADF KAAGAQLVGT 

        70         80         90        100        110        120 
ADQVWADADL LLKVKEPIAA EYGRLRHGQI LFTFLHLAAS RACTDALLDS GTTSIAYETV 

       130        140        150        160        170        180 
QTADGALPLL APMSEVAGRL AAQVGAYHLM RTQGGRGVLM GGVPGVEPAD VVVIGAGTAG 

       190        200        210        220        230        240 
YNAARIANGM GATVTVLDIN IDKLRQLDAE FCGRIHTRYS SAYELEGAVK RADLVIGAVL 

       250        260        270        280        290        300 
VPGAKAPKLV SNSLVAHMKP GAVLVDIAID QGGCFEGSRP TTYDHPTFAV HDTLFYCVAN 

       310        320        330        340        350        360 
MPASVPKTST YALTNATMPY VLELADHGWR AACRSNPALA KGLSTHEGAL LSERVATDLG 

       370 
VPFTEPASVL A

P30234 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