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Q52998 (TDH_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-threonine 3-dehydrogenase
EC=1.1.1.103
Gene names
Name:tdh
Ordered Locus Names:R02315
ORF Names:SMc01564
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. HAMAP MF_00627

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00627

Pathway

Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2. HAMAP MF_00627

Subunit structure

Homotetramer By similarity. HAMAP MF_00627

Subcellular location

Cytoplasm By similarity HAMAP MF_00627.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processthreonine catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-threonine 3-dehydrogenase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344L-threonine 3-dehydrogenase HAMAP MF_00627
PRO_0000160851

Sites

Metal binding421Zinc 1; catalytic By similarity
Metal binding671Zinc 1; catalytic By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding1521Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q52998 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 75642C3D084B2C2F

FASTA34437,569
        10         20         30         40         50         60 
MTNMMKALVK TKPEVGLWME RVPVPEIGPN DVLIRVRKSA ICGTDVHIWN WDQWAEKTIP 

        70         80         90        100        110        120 
VPMVVGHEFM GEVVEVGPAV SKHHVGERVS GEGHIVCGKC RNCRAGRGHL CRNTLGVGVN 

       130        140        150        160        170        180 
RPGSFAEFVC LPEYNVVSIP DDVPDEIAAI FDPFGNAVHT ALSFDLVGED VLVTGAGPIG 

       190        200        210        220        230        240 
IMGAMVAKRC GARKVVITDI NPVRLDLARK LGIDHVVDAS KEKLADVMRV IGMTEGFDVG 

       250        260        270        280        290        300 
LEMSGAAPAF RDMIDKMNNG GKIAILGIAP AGFEIDWNKV IFKMLNLKGI YGREMFETWY 

       310        320        330        340 
KMIAFVQGGL DLSPIITHRI GIDDFRDGFE AMRSGNSGKV VMDW

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[2]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"Cloning and characterization of the sigA gene encoding the major sigma subunit of Rhizobium meliloti."
Rushing B.G., Long S.R.
J. Bacteriol. 177:6952-6957(1995) [PubMed: 7592490] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-344.
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL591688 Genomic DNA. Translation: CAC46894.1.
L47288 Genomic DNA. Translation: AAA88523.1.
RefSeqNP_386421.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ52998.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1233982.
GenomeReviewsGene locus R02315 in contig AL591688_GR.
KEGGsme:SMc01564.
NMPDRfig|266834.1.peg.3609.
PATRIC23634111. VBISinMel96828_3793.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753318.
OMARDGFEAM.
ProtClustDBPRK05396.

Enzyme and pathway databases

BioCycSMEL266834:SMC01564-MONOMER.

Family and domain databases

HAMAPMF_00627. Thr_dehydrog.
[Tree]
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR004627. L-Threonine_3-DHase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00060.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
TIGRFAMsTIGR00692. Tdh. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTDH_RHIME
AccessionPrimary (citable) accession number: Q52998
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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