P0A2W8 (ALR_STRPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine racemase
EC=5.1.1.1

Gene names

Name:	alr
Synonyms:	alaR
Ordered Locus Names:	SP_1698

Organism

Streptococcus pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP MF_01201
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01201
Pathway	Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP 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	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	alanine metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 – 367

367

Alanine racemase HAMAP MF_01201

PRO_0000114581

Sites

Active site

40

1

Proton acceptor; specific for D-alanine By similarity

Active site

263

1

Proton acceptor; specific for L-alanine By similarity

Amino acid modifications

Modified residue

40

1

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

354

1

V → E in CAA90279. Ref.3

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

10 – 14

5

Helix

18 – 24

7

Beta strand

34 – 38

5

Helix

40 – 43

4

Helix

49 – 55

7

Helix

56 – 58

3

Beta strand

63 – 66

4

Helix

67 – 75

9

Helix

90 – 92

3

Helix

93 – 98

6

Beta strand

102 – 105

4

Helix

109 – 116

8

Beta strand

125 – 130

6

Helix

142 – 154

13

Helix

175 – 189

15

Beta strand

199 – 201

3

Helix

203 – 208

6

Helix

210 – 212

3

Beta strand

215 – 219

5

Beta strand

243 – 248

6

Beta strand

250 – 255

6

Beta strand

273 – 278

6

Helix

288 – 290

3

Beta strand

294 – 296

3

Beta strand

301 – 304

4

Beta strand

313 – 319

7

Beta strand

326 – 330

5

Helix

340 – 347

8

Helix

351 – 356

6

Beta strand

364 – 367

4

Sequences

	Sequence		Length	Mass (Da)
	P0A2W8 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: A79E2F1B439B18B7	FASTA	367	39,858
	10 20 30 40 50 60 MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA VAKAIQDDVD 70 80 90 100 110 120 GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD FTLTVAGLEW IQALLDKEVD 130 140 150 160 170 180 LTGLTVHLKI DSGMGRIGFR EASEVEQAQD LLQQHGVCVE GIFTHFATAD EESDDYFNAQ 190 200 210 220 230 240 LERFKTILAS MKEVPELVHA SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI 250 260 270 280 290 300 PALTLESALV HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ 310 320 330 340 350 360 ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI NYEVVCLLSD RIPREYY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Guynn L.J., Strych U., Benedik M.J. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M. Science 293:498-506(2001) [PubMed: 11463916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4.
[3]	"The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination." Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P. Mol. Microbiol. 19:1035-1045(1996) [PubMed: 8830261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-367.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF171873 Genomic DNA. Translation: AAD51027.1.
AE005672 Genomic DNA. Translation: AAK75776.1.
Z49988 Genomic DNA. Translation: CAA90279.1.

PIR

G95197.
S71015.

RefSeq

NP_346136.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3S46	X-ray	2.00	A/B	1-367	[»]

ProteinModelPortal

P0A2W8.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBSTRT00000025965; EBSTRP00000025057; EBSTRG00000025965.

GeneID

931137.

GenomeReviews

Gene locus SP_1698 in contig AE005672_GR.

KEGG

spn:SP_1698.

PATRIC

19707839. VBIStrPne105772_1762.

TIGR

SP_1698.

Phylogenomic databases

GeneTree

EBGT00050000028408.

HOGENOM

HBG712172.

OMA

TRKEDAN.

ProtClustDB

PRK00053.

Enzyme and pathway databases

BioCyc

SPNE170187-1:SP_1698-MONOMER.

BRENDA

5.1.1.1. 5946.

Family and domain databases

HAMAP

MF_01201. Ala_racemase.
[Tree]

InterPro

IPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]

Gene3D

G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit.

KO

K01775.

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

ALR_STRPN

Accession

Primary (citable) accession number: P0A2W8
Secondary accession number(s): Q54899, Q9S3V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program