Alanine racemase, biosynthetic - Agrobacterium tumefaciens (strain C58 / ATCC 33970)

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P58736 (ALR1_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alanine racemase, biosynthetic
EC=5.1.1.1

Gene names

Name:	alr
Ordered Locus Names:	Atu1080
ORF Names:	AGR_C_1996

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium › Agrobacterium tumefaciens complex ›

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP-Rule MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP-Rule MF_01201
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_01201
Sequence similarities	Belongs to the alanine racemase family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alanine racemase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 391

391

Alanine racemase, biosynthetic HAMAP-Rule MF_01201

PRO_0000114492

Sites

Active site

Proton acceptor; specific for D-alanine By similarity

Active site

271

Proton acceptor; specific for L-alanine By similarity

Binding site

149

Substrate By similarity

Binding site

330

Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P58736 [UniParc].

Last modified March 5, 2002. Version 1.
Checksum: 82F6B0320F92B770
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FASTA

391

42,091

        10         20         30         40         50         60 
MTDDFEDSFP DNETDAFEQA PLRLTVDLGA LADNWRDMKK RSGRARTAAV VKADAYGLGI 

        70         80         90        100        110        120 
EDCGATLYHA GARDFFVATV AEGATLRSYA PEARIFVLSG IWQGQERQVF DNDLVPVLAS 

       130        140        150        160        170        180 
EEQLSFWMAT VAERGDHPCA LHVDTGFNRL GLPLDDALFL ADDVTRPASF DPVLVLSHLA 

       190        200        210        220        230        240 
CADTPSSPMN RAQLESFRRV SAAFEGIESS LSASAGIFLG PDYHFDLTRP GIALYGGEAV 

       250        260        270        280        290        300 
NDVANPMRPV AKAEARIIQI REAGEGQTVS YGSSFLLKRA SRLAIASVGY ADGYQRSLSG 

       310        320        330        340        350        360 
SGIPLREMGH GGAYGVVNGH KVPVAGRVTM DLTIFDVTDV PANAIRAGDY IELFGPNVPV 

       370        380        390 
DETARAAGTI GYEMLTGLGL RYERQYLVAD D

« Hide

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58."
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J.

Nester E.W.
Science 294:2317-2323(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58."
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C.

Slater S.
Science 294:2323-2328(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK86889.1.
PIR	AG2709. H97491.
RefSeq	NP_354104.1. NC_003062.2.
3D structure databases
ProteinModelPortal	P58736.
ModBase	Search...
Protein-protein interaction databases
STRING	176299.Atu1080.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1133118.
KEGG	atu:Atu1080.
PATRIC	20811909. VBIAgrTum91616_1095.
Phylogenomic databases
eggNOG	COG0787.
HOGENOM	HOG000031445.
KO	K01775.
OMA	GDYIELF.
ProtClustDB	CLSK800293.
Enzyme and pathway databases
UniPathway	UPA00042; UER00497. UPA00219.
Family and domain databases
Gene3D	2.40.37.10. 1 hit.
HAMAP	MF_01201. Ala_racemase.
InterPro	IPR000821. Ala_racemase. IPR009006. Ala_racemase/Decarboxylase_C. IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR020622. Ala_racemase_pyridoxalP-BS. [Graphical view]
Pfam	PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view]
PRINTS	PR00992. ALARACEMASE.
SMART	SM01005. Ala_racemase_C. 1 hit. [Graphical view]
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMs	TIGR00492. alr. 1 hit.
PROSITE	PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALR1_AGRT5

Accession

Primary (citable) accession number: P58736

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 5, 2002
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents