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E4Q797 (E4Q797_CALH1) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 RuleBase RU000608 SAAS SAAS020622

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. RuleBase RU004247 HAMAP-Rule MF_01201 SAAS SAAS020622

Sequence similarities

Belongs to the alanine racemase family. RuleBase RU004188 HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site411Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2701Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1391Substrate By similarity HAMAP-Rule MF_01201
Binding site3181Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
E4Q797 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 1E6D81719C1ABC8D

FASTA39044,046
        10         20         30         40         50         60 
MNKLSLYNRV WAEIDLDNLV YNLENIKKKI LPQTHIMAVV KADAYGHGAV EISRVLVKNG 

        70         80         90        100        110        120 
VSMLAVAIID EALQLRHFNF DVPILILGFT PFELSEQVVE NEISQTVYTY EQAYYLSQAA 

       130        140        150        160        170        180 
QKVGKKAKIH IKVDTGMGRI GFLCCDESIQ TVLNIAKLPN IELEGIFSHF SSADDPDSDN 

       190        200        210        220        230        240 
FTHEQFMKFE NFVKELNKNG VYFKYKHIAN SSAAIRFPQY QLDVVRLGLI LYGLYPNSSL 

       250        260        270        280        290        300 
KEHISIKPVM SVKARVINVK EVPEGFPISY NRRYITTRKS KIATIPIGYA DGFTRVGSSQ 

       310        320        330        340        350        360 
RHVLIKGEFA KVVGSICMDQ CMVDVTDIED VKIGDEVVII GKQGKNEILA DHLAEQIGTI 

       370        380        390 
NYEIVCSFSK RIPRVYIKDG RVVKILNYIL

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Caldicellulosiruptor hydrothermalis 108."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N. expand/collapse author list , Blumer-Schuette S.E., Kelly R.M., Woyke T.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 108.
[2]"Complete genome sequences for the anaerobic, extremely thermophilic plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis, Caldicellulosiruptor owensensis, and Caldicellulosiruptor lactoaceticus."
Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.
J. Bacteriol. 193:1483-1484(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18901 / VKM B-2411 / 108.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002219 Genomic DNA. Translation: ADQ06610.1.
RefSeqYP_003991979.1. NC_014652.1.

3D structure databases

ProteinModelPortalE4Q797.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADQ06610; ADQ06610; Calhy_0881.
GeneID9935412.
KEGGchd:Calhy_0881.
PATRIC42585338. VBICalHyd101559_0951.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMAPTLCNPQ.

Enzyme and pathway databases

BioCycCHYD632292:GHA8-905-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4Q797_CALH1
AccessionPrimary (citable) accession number: E4Q797
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: May 29, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info