Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alanine racemase

Gene

alr

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine.2 Publications

Catalytic activityi

L-alanine = D-alanine.UniRule annotation3 Publications

Cofactori

pyridoxal 5'-phosphateUniRule annotation6 Publications

Enzyme regulationi

Inhibited by acetate and propionate. Irreversibly inhibited by cycloserine.3 Publications

Pathwayi: D-alanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-alanine from L-alanine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Alanine racemase (AA904_04350), Alanine racemase (alr), Alanine racemase (GT94_03080), Alanine racemase (alr)
This subpathway is part of the pathway D-alanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-alanine from L-alanine, the pathway D-alanine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei39Proton acceptor; specific for D-alanine2 Publications1
Binding sitei136Substrate1 Publication1
Active sitei265Proton acceptor; specific for L-alanine2 Publications1
Binding sitei312Substrate; via amide nitrogen1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.1.1.1. 623.
SABIO-RKP10724.
UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemaseUniRule annotation (EC:5.1.1.1UniRule annotation3 Publications)
Gene namesi
Name:alr
Synonyms:dal
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39K → A: Loss of activity. 1 Publication1
Mutagenesisi166H → A: 6.5-fold decrease in activity. 1 Publication1
Mutagenesisi219R → A: 100-fold decrease in activity. 1 Publication1
Mutagenesisi219R → E: 1000-fold decrease in activity. 1 Publication1
Mutagenesisi219R → K: 4-fold decrease in activity. 1 Publication1
Mutagenesisi265Y → A: 5000-fold decrease in activity. 1 Publication1
Mutagenesisi265Y → F: Loss of activity. 1 Publication1
Mutagenesisi265Y → S: 2000-fold decrease in activity. 1 Publication1
Mutagenesisi354Y → A: 54-fold increase in serine racemase activity. 1 Publication1
Mutagenesisi354Y → N: 81-fold increase in serine racemase activity. 1 Publication1
Mutagenesisi354Y → Q: 51-fold increase in serine racemase activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001144991 – 388Alanine racemaseAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei39N6-(pyridoxal phosphate)lysine3 Publications1
Modified residuei129N6-carboxylysine5 Publications1

Interactioni

Subunit structurei

Homodimer.5 Publications

Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Helixi14 – 27Combined sources14
Beta strandi33 – 37Combined sources5
Helixi39 – 43Combined sources5
Helixi47 – 57Combined sources11
Beta strandi61 – 66Combined sources6
Helixi67 – 75Combined sources9
Beta strandi82 – 84Combined sources3
Helixi90 – 92Combined sources3
Helixi93 – 98Combined sources6
Beta strandi101 – 105Combined sources5
Helixi108 – 117Combined sources10
Beta strandi124 – 130Combined sources7
Beta strandi132 – 134Combined sources3
Beta strandi136 – 139Combined sources4
Helixi142 – 154Combined sources13
Beta strandi158 – 164Combined sources7
Beta strandi172 – 174Combined sources3
Helixi176 – 189Combined sources14
Beta strandi192 – 194Combined sources3
Beta strandi197 – 200Combined sources4
Helixi204 – 209Combined sources6
Helixi211 – 213Combined sources3
Beta strandi217 – 220Combined sources4
Helixi222 – 225Combined sources4
Helixi231 – 236Combined sources6
Beta strandi245 – 250Combined sources6
Beta strandi252 – 257Combined sources6
Beta strandi262 – 264Combined sources3
Helixi265 – 267Combined sources3
Beta strandi273 – 281Combined sources9
Helixi284 – 286Combined sources3
Helixi290 – 294Combined sources5
Beta strandi296 – 299Combined sources4
Beta strandi302 – 308Combined sources7
Beta strandi315 – 318Combined sources4
Beta strandi328 – 335Combined sources8
Beta strandi338 – 340Combined sources3
Helixi342 – 349Combined sources8
Helixi355 – 359Combined sources5
Beta strandi366 – 370Combined sources5
Beta strandi373 – 378Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BD0X-ray1.60A/B1-388[»]
1EPVX-ray2.20A/B2-388[»]
1FTXX-ray2.20A/B2-388[»]
1L6FX-ray2.00A/B1-388[»]
1L6GX-ray2.00A/B1-388[»]
1NIUX-ray2.20A/B1-388[»]
1SFTX-ray1.90A/B1-388[»]
1XQKX-ray1.95A/B1-382[»]
1XQLX-ray1.80A/B1-382[»]
2SFPX-ray1.90A/B1-388[»]
3UW6X-ray2.30A/B/C1-388[»]
4ILSX-ray2.50A/B/C1-388[»]
ProteinModelPortaliP10724.
SMRiP10724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10724.

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotation

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase. 1 hit.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10724-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDFHRDTWA EVDLDAIYDN VENLRRLLPD DTHIMAVVKA NAYGHGDVQV
60 70 80 90 100
ARTALEAGAS RLAVAFLDEA LALREKGIEA PILVLGASRP ADAALAAQQR
110 120 130 140 150
IALTVFRSDW LEEASALYSG PFPIHFHLKM DTGMGRLGVK DEEETKRIVA
160 170 180 190 200
LIERHPHFVL EGLYTHFATA DEVNTDYFSY QYTRFLHMLE WLPSRPPLVH
210 220 230 240 250
CANSAASLRF PDRTFNMVRF GIAMYGLAPS PGIKPLLPYP LKEAFSLHSR
260 270 280 290 300
LVHVKKLQPG EKVSYGATYT AQTEEWIGTI PIGYADGWLR RLQHFHVLVD
310 320 330 340 350
GQKAPIVGRI CMDQCMIRLP GPLPVGTKVT LIGRQGDEVI SIDDVARHLE
360 370 380
TINYEVPCTI SYRVPRIFFR HKRIMEVRNA IGRGESSA
Length:388
Mass (Da):43,593
Last modified:November 1, 1997 - v2
Checksum:iF54AA581F135EA7A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37 – 38VV → PP AA sequence (PubMed:3730360).Curated2
Sequence conflicti57 – 62AGASRL → RGPPP in AAA22220 (PubMed:2835089).Curated6
Sequence conflicti288 – 289WL → V in AAA22220 (PubMed:2835089).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19142 Genomic DNA. Translation: AAA22220.1.
PIRiA29984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19142 Genomic DNA. Translation: AAA22220.1.
PIRiA29984.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BD0X-ray1.60A/B1-388[»]
1EPVX-ray2.20A/B2-388[»]
1FTXX-ray2.20A/B2-388[»]
1L6FX-ray2.00A/B1-388[»]
1L6GX-ray2.00A/B1-388[»]
1NIUX-ray2.20A/B1-388[»]
1SFTX-ray1.90A/B1-388[»]
1XQKX-ray1.95A/B1-382[»]
1XQLX-ray1.80A/B1-382[»]
2SFPX-ray1.90A/B1-388[»]
3UW6X-ray2.30A/B/C1-388[»]
4ILSX-ray2.50A/B/C1-388[»]
ProteinModelPortaliP10724.
SMRiP10724.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1075086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.
BRENDAi5.1.1.1. 623.
SABIO-RKP10724.

Miscellaneous databases

EvolutionaryTraceiP10724.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase. 1 hit.
InterProiIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSiPR00992. ALARACEMASE.
SMARTiSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR00492. alr. 1 hit.
PROSITEiPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALR_GEOSE
AccessioniPrimary (citable) accession number: P10724
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.