N-acylamino acid racemase - Deinococcus radiodurans

Preferred order of sections

Names and origin

Protein names

Submitted name:
N-acylamino acid racemase EMBL AAF09631.1

Gene names

Ordered Locus Names:

DR_0044

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Magnesium PDB 2GGH PDB 1XPY PDB 1XS2 Metal-binding SAAS SAAS013342 PDB 2GGH PDB 1XPY PDB 1XS2
Technical term	3D-structure PDB 1R0M PDB 2GGH PDB 2FKP PDB 2GGJ PDB 2GGG PDB 2GGI PDB 1XPY PDB 1XS2 Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	catalytic activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

168

1

Magnesium PDB 2GGH

Metal binding

195

1

Magnesium PDB 2GGH

Metal binding

220

1

Magnesium PDB 2GGH

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RYA6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 62F68CFA9FEF3DA4
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FASTA

375

40,901

        10         20         30         40         50         60 
MAHTGRMFKI EAAEIVVARL PLKFRFETSF GVQTHKVVPL LILHGEGVQG VAEGTMEARP 

        70         80         90        100        110        120 
MYREETIAGA LDLLRGTFLP AILGQTFANP EAVADALGSY RGNRMARAMV EMAAWDLWAR 

       130        140        150        160        170        180 
TLGVPLGTLL GGHKEQVEVG VSLGIQAGEQ ATVDLVRKHV EQGYRRIKLK IKPGWDVQPV 

       190        200        210        220        230        240 
RATREAFPDI RLTVDANSAY TLADAGRLRQ LDEYDLTYIE QPLAWDDLVD HAELARRIRT 

       250        260        270        280        290        300 
PLCLDESVAS AADARKALAL GAGGVINLKV ARVGGHAESR RVHDVAQSFG APVWCGGMLE 

       310        320        330        340        350        360 
SGIGRAHNIH LSTLPNFRLP GDTSSASRYW ERDLIQEPLE AVDGLMPVPQ GPGTGVTLDR 

       370 
EFLATVTEAQ EEHRA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans." Wang W.C., Chiu W.C., Hsu S.K., Wu C.L., Chen C.Y., Liu J.S., Hsu W.H. J. Mol. Biol. 342:155-169(2004) [PubMed: 15313614] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS).
[3]	"Enhanced thermoactivity in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase but not in N-acylamino acid racemase that has induced fit movements upon substrate binding." Wang W.C., Chiu W.C. Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[4]	"Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase." Chiu W.C., You J.Y., Liu J.S., Hsu S.K., Hsu W.H., Shih C.H., Hwang J.K., Wang W.C. J. Mol. Biol. 359:741-753(2006) [PubMed: 16650857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000513 Genomic DNA. Translation: AAF09631.1.

PIR

D75568.

RefSeq

NP_293770.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R0M	X-ray	1.30	A/B/C/D	1-375	[»]
1XPY	X-ray	2.30	A/B/C/D	1-375	[»]
1XS2	X-ray	2.30	A/B/C/D	1-375	[»]
2FKP	X-ray	2.00	A/B/C/D	1-375	[»]
2GGG	X-ray	2.40	A/B/C/D	1-375	[»]
2GGH	X-ray	2.20	A/B/C/D	1-375	[»]
2GGI	X-ray	2.20	A/B/C/D	1-375	[»]
2GGJ	X-ray	2.50	A/B/C/D	1-375	[»]

ProteinModelPortal

Q9RYA6.

SMR

Q9RYA6. Positions 6-375.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1799680.

GenomeReviews

Gene locus DR_0044 in contig AE000513_GR.

KEGG

dra:DR_0044.

NMPDR

fig|243230.1.peg.229.

PATRIC

21627561. VBIDeiRad64572_0209.

TIGR

DR_0044.

Phylogenomic databases

HOGENOM

HBG292917.

OMA

CHISEYV.

ProtClustDB

CLSK862528.

Family and domain databases

InterPro

IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
IPR010197. OSB_synthase_lowGC-bac/arc.
[Graphical view]

KO

K02549.

PANTHER

PTHR13794:SF8. MenC_lowGC_arc. 1 hit.
PTHR13794. MR_MLE. 1 hit.

Pfam

PF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]

SMART

SM00922. MR_MLE. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01928. MenC_lowGC/arch. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q9RYA6_DEIRA

Accession

Primary (citable) accession number: Q9RYA6

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)