Q9HTQ2 (ALR2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine racemase, catabolic
EC=5.1.1.1

Gene names

Name:	dadX
Ordered Locus Names:	PA5302

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. HAMAP-Rule MF_01201
Catalytic activity	L-alanine = D-alanine. HAMAP-Rule MF_01201
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the alanine racemase family.
Biophysicochemical properties	Kinetic parameters: KM=1.40 mM for D-alanine KM=1.40 mM for L-alanine Vmax=134 µmol/min/mg enzyme toward D-alanine Vmax=155 µmol/min/mg enzyme toward L-alanine

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-alanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 357

357

Alanine racemase, catabolic HAMAP-Rule MF_01201

PRO_0000114547

Sites

Active site

33

1

Proton acceptor; specific for D-alanine

Active site

253

1

Proton acceptor; specific for L-alanine

Binding site

129

1

Substrate

Binding site

301

1

Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue

33

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_01201

Modified residue

122

1

N6-carboxylysine

Experimental info

Sequence conflict

138

1

S → R in AAD47081. Ref.1

Sequence conflict

178

1

A → S in AAD47081. Ref.1

Sequence conflict

262

1

S → R in AAD47081. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

357

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

10 – 24

15

Beta strand

26 – 31

6

Helix

33 – 37

5

Helix

41 – 48

8

Turn

49 – 51

3

Beta strand

53 – 59

7

Helix

60 – 68

9

Beta strand

75 – 77

3

Helix

84 – 86

3

Helix

87 – 92

6

Beta strand

95 – 99

5

Helix

102 – 110

9

Beta strand

117 – 123

7

Beta strand

125 – 127

3

Beta strand

129 – 132

4

Helix

134 – 146

13

Beta strand

150 – 156

7

Helix

169 – 181

13

Helix

193 – 198

6

Beta strand

205 – 207

3

Helix

211 – 214

4

Beta strand

218 – 221

4

Helix

226 – 228

3

Beta strand

233 – 245

13

Beta strand

250 – 252

3

Helix

253 – 255

3

Beta strand

260 – 269

10

Helix

272 – 274

3

Beta strand

285 – 288

4

Beta strand

291 – 295

5

Beta strand

304 – 307

4

Beta strand

319 – 327

9

Helix

329 – 335

7

Helix

340 – 345

6

Beta strand

352 – 355

4

Sequences

	Sequence		Length	Mass (Da)
	Q9HTQ2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 199F4021D02FFF48	FASTA	357	38,915
	10 20 30 40 50 60 MRPARALIDL QALRHNYRLA REATGARALA VIKADAYGHG AVRCAEALAA EADGFAVACI 70 80 90 100 110 120 EEGLELREAG IRQPILLLEG FFEASELELI VAHDFWCVVH CAWQLEAIER ASLARPLNVW 130 140 150 160 170 180 LKMDSGMHRV GFFPEDFSAA HERLRASGKV AKIVMMSHFS RADELDCPRT EEQLAAFAAA 190 200 210 220 230 240 SQGLEGEISL RNSPAVLGWP KVPSDWVRPG ILLYGATPFE RAHPLADRLR PVMTLESKVI 250 260 270 280 290 300 SVRDLPAGEP VGYGARYSTE RSQRIGVVAM GYADGYPRHA ADGTLVFIDG KPGRLVGRVS 310 320 330 340 350 MDMLTVDLTD HPQAGLGSRV ELWGPNVPVG ALAAQFGSIP YQLLCNLKRV PRVYSGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1." Strych U., Huang H.-C., Krause K.L., Benedik M.J. Curr. Microbiol. 41:290-294(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]	"Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms." LeMagueres P., Im H., Dvorak A., Strych U., Benedik M.J., Krause K.L. Biochemistry 42:14752-14761(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND LYSINE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-33, CARBOXYLATION AT LYS-122.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF165881 Genomic DNA. Translation: AAD47081.1.
AE004091 Genomic DNA. Translation: AAG08687.1.

PIR

F82982.

RefSeq

NP_253989.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RCQ	X-ray	1.45	A	1-357	[»]

ProteinModelPortal

Q9HTQ2.

SMR

Q9HTQ2. Positions 1-357.

ModBase

Search...

Protein-protein interaction databases

STRING

208964.PA5302.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

878055.

KEGG

pae:PA5302.

PATRIC

19845459. VBIPseAer58763_5556.

Organism-specific databases

PseudoCAP

PA5302.

Phylogenomic databases

eggNOG

COG0787.

HOGENOM

HOG000031446.

KO

K01775.

OMA

HQLETAV.

ProtClustDB

PRK03646.

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...

Other

EvolutionaryTrace

Q9HTQ2.

Entry information

Entry name

ALR2_PSEAE

Accession

Primary (citable) accession number: Q9HTQ2
Secondary accession number(s): Q9S419

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program