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Protein

Alanine racemase 2

Gene

alr2

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.UniRule annotation

Catalytic activityi

L-alanine = D-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: 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 1 (alr1), Alanine racemase 2 (alr2)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei59 – 591Proton acceptor; specific for D-alanineUniRule annotation
Binding sitei158 – 1581SubstrateUniRule annotation
Active sitei284 – 2841Proton acceptor; specific for L-alanineUniRule annotation
Binding sitei332 – 3321Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

  • alanine racemase activity Source: TIGR
  • pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  • D-alanine biosynthetic process Source: UniProtKB-UniPathway
  • peptidoglycan biosynthetic process Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine racemase 2UniRule annotation (EC:5.1.1.1UniRule annotation)
Gene namesi
Name:alr2
Ordered Locus Names:VC_1312
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Alanine racemase 2PRO_0000114592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1312.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 245Combined sources
Beta strandi26 – 338Combined sources
Helixi34 – 4512Combined sources
Beta strandi54 – 574Combined sources
Helixi59 – 635Combined sources
Helixi67 – 7610Combined sources
Beta strandi81 – 866Combined sources
Helixi87 – 959Combined sources
Beta strandi100 – 1045Combined sources
Helixi110 – 1156Combined sources
Helixi117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Helixi128 – 14114Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi158 – 1614Combined sources
Helixi166 – 17611Combined sources
Beta strandi181 – 1877Combined sources
Helixi195 – 21521Combined sources
Helixi220 – 2223Combined sources
Beta strandi224 – 2285Combined sources
Helixi230 – 2356Combined sources
Helixi237 – 2393Combined sources
Turni248 – 2525Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi281 – 2833Combined sources
Helixi284 – 2863Combined sources
Beta strandi294 – 3007Combined sources
Helixi303 – 3053Combined sources
Helixi309 – 3113Combined sources
Turni312 – 3143Combined sources
Beta strandi316 – 3194Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi335 – 3384Combined sources
Beta strandi350 – 3578Combined sources
Helixi364 – 3718Combined sources
Helixi375 – 38511Combined sources
Beta strandi388 – 3914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BEQX-ray1.50A9-392[»]
4BEUX-ray1.15A9-392[»]
ProteinModelPortaliQ9KSE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alanine racemase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0787.
OMAiNTVMVDV.
OrthoDBiEOG6PP9NJ.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
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.

Q9KSE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSFSLSAAP LHIDTALPDA AQIQQSNSWL EISLGQFQSN IEQFKSHMNA
60 70 80 90 100
NTKICAIMKA DAYGNGIRGL MPTIIAQGIP CVGVASNAEA RAVRESGFKG
110 120 130 140 150
ELIRVRSASL SEMSSALDLN IEELIGTHQQ ALDLAELAKQ SGKTLKVHIA
160 170 180 190 200
LNDGGMGRNG IDMTTEAGKK EAVSIATQPS LSVVGIMTHF PNYNADEVRA
210 220 230 240 250
KLAQFKESST WLMQQANLKR EEITLHVANS YTALNVPEAQ LDMVRPGGVL
260 270 280 290 300
FGDLPTNPEY PSIVSFKTRV SSLHHLPKDS TVGYDSTFTT SRDSVLANLP
310 320 330 340 350
VGYSDGYPRK MGNKAEVLIN GQRAKVVGVT SMNTTVVDVT EIKGVLPGQE
360 370 380 390
VVLFGQQQKQ SIAVSEMENN AELIFPELYT LWGTSNPRFY VK
Length:392
Mass (Da):42,498
Last modified:March 5, 2002 - v2
Checksum:iC0211DC2661691FD
GO

Sequence cautioni

The sequence AAF94470.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94470.1. Different initiation.
PIRiA82215.

Genome annotation databases

EnsemblBacteriaiAAF94470; AAF94470; VC_1312.
PATRICi20081706. VBIVibCho83274_1252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94470.1. Different initiation.
PIRiA82215.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BEQX-ray1.50A9-392[»]
4BEUX-ray1.15A9-392[»]
ProteinModelPortaliQ9KSE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1312.

Protocols and materials databases

DNASUi2614766.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF94470; AAF94470; VC_1312.
PATRICi20081706. VBIVibCho83274_1252.

Phylogenomic databases

eggNOGiCOG0787.
OMAiNTVMVDV.
OrthoDBiEOG6PP9NJ.

Enzyme and pathway databases

UniPathwayiUPA00042; UER00497.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPiMF_01201. Ala_racemase.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiALR2_VIBCH
AccessioniPrimary (citable) accession number: Q9KSE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 27, 2015
This is version 96 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, Complete proteome, Reference proteome

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

External Data

Dasty 3

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 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.