Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10724

- ALR_GEOSE

UniProt

P10724 - ALR_GEOSE

Protein

Alanine racemase

Gene

alr

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

    L-alanine = D-alanine.3 PublicationsUniRule annotation

    Cofactori

    Pyridoxal phosphate.6 PublicationsUniRule annotation

    Enzyme regulationi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei39 – 391Proton acceptor; specific for D-alanine
    Binding sitei136 – 1361Substrate
    Active sitei265 – 2651Proton acceptor; specific for L-alanine
    Binding sitei312 – 3121Substrate; via amide nitrogen

    GO - Molecular functioni

    1. alanine racemase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. D-alanine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    SABIO-RKP10724.
    UniPathwayiUPA00042; UER00497.

    Names & Taxonomyi

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391K → A: Loss of activity. 1 Publication
    Mutagenesisi166 – 1661H → A: 6.5-fold decrease in activity. 1 Publication
    Mutagenesisi219 – 2191R → A: 100-fold decrease in activity. 2 Publications
    Mutagenesisi219 – 2191R → E: 1000-fold decrease in activity. 2 Publications
    Mutagenesisi219 – 2191R → K: 4-fold decrease in activity. 2 Publications
    Mutagenesisi265 – 2651Y → A: 5000-fold decrease in activity. 2 Publications
    Mutagenesisi265 – 2651Y → F: Loss of activity. 2 Publications
    Mutagenesisi265 – 2651Y → S: 2000-fold decrease in activity. 2 Publications
    Mutagenesisi354 – 3541Y → A: 54-fold increase in serine racemase activity. 2 Publications
    Mutagenesisi354 – 3541Y → N: 81-fold increase in serine racemase activity. 2 Publications
    Mutagenesisi354 – 3541Y → Q: 51-fold increase in serine racemase activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 388388Alanine racemasePRO_0000114499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391N6-(pyridoxal phosphate)lysine
    Modified residuei129 – 1291N6-carboxylysine5 Publications

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Structurei

    Secondary structure

    1
    388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 138
    Helixi14 – 2714
    Beta strandi33 – 375
    Helixi39 – 435
    Helixi47 – 5711
    Beta strandi61 – 666
    Helixi67 – 759
    Beta strandi82 – 843
    Helixi90 – 923
    Helixi93 – 986
    Beta strandi101 – 1055
    Helixi108 – 11710
    Beta strandi124 – 1307
    Beta strandi132 – 1343
    Beta strandi136 – 1394
    Helixi142 – 15413
    Beta strandi158 – 1647
    Beta strandi172 – 1743
    Helixi176 – 18914
    Beta strandi192 – 1943
    Beta strandi197 – 2004
    Helixi204 – 2096
    Helixi211 – 2133
    Beta strandi217 – 2204
    Helixi222 – 2254
    Helixi231 – 2366
    Beta strandi245 – 2506
    Beta strandi252 – 2576
    Beta strandi262 – 2643
    Helixi265 – 2673
    Beta strandi273 – 2819
    Helixi284 – 2863
    Helixi290 – 2945
    Beta strandi296 – 2994
    Beta strandi302 – 3087
    Beta strandi315 – 3184
    Beta strandi328 – 3358
    Beta strandi338 – 3403
    Helixi342 – 3498
    Helixi355 – 3595
    Beta strandi366 – 3705
    Beta strandi373 – 3786

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-382.
    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.
    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

    MNDFHRDTWA EVDLDAIYDN VENLRRLLPD DTHIMAVVKA NAYGHGDVQV    50
    ARTALEAGAS RLAVAFLDEA LALREKGIEA PILVLGASRP ADAALAAQQR 100
    IALTVFRSDW LEEASALYSG PFPIHFHLKM DTGMGRLGVK DEEETKRIVA 150
    LIERHPHFVL EGLYTHFATA DEVNTDYFSY QYTRFLHMLE WLPSRPPLVH 200
    CANSAASLRF PDRTFNMVRF GIAMYGLAPS PGIKPLLPYP LKEAFSLHSR 250
    LVHVKKLQPG EKVSYGATYT AQTEEWIGTI PIGYADGWLR RLQHFHVLVD 300
    GQKAPIVGRI CMDQCMIRLP GPLPVGTKVT LIGRQGDEVI SIDDVARHLE 350
    TINYEVPCTI SYRVPRIFFR HKRIMEVRNA IGRGESSA 388
    Length:388
    Mass (Da):43,593
    Last modified:November 1, 1997 - v2
    Checksum:iF54AA581F135EA7A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 382VV → PP AA sequence (PubMed:3730360)Curated
    Sequence conflicti57 – 626AGASRL → RGPPP in AAA22220. (PubMed:2835089)Curated
    Sequence conflicti288 – 2892WL → V in AAA22220. (PubMed:2835089)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19142 Genomic DNA. Translation: AAA22220.1.
    PIRiA29984.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19142 Genomic DNA. Translation: AAA22220.1 .
    PIRi A29984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BD0 X-ray 1.60 A/B 1-388 [» ]
    1EPV X-ray 2.20 A/B 2-388 [» ]
    1FTX X-ray 2.20 A/B 2-388 [» ]
    1L6F X-ray 2.00 A/B 1-388 [» ]
    1L6G X-ray 2.00 A/B 1-388 [» ]
    1NIU X-ray 2.20 A/B 1-388 [» ]
    1SFT X-ray 1.90 A/B 1-388 [» ]
    1XQK X-ray 1.95 A/B 1-382 [» ]
    1XQL X-ray 1.80 A/B 1-382 [» ]
    2SFP X-ray 1.90 A/B 1-388 [» ]
    3UW6 X-ray 2.30 A/B/C 1-388 [» ]
    4ILS X-ray 2.50 A/B/C 1-388 [» ]
    ProteinModelPortali P10724.
    SMRi P10724. Positions 2-382.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1075086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00042 ; UER00497 .
    SABIO-RK P10724.

    Miscellaneous databases

    EvolutionaryTracei P10724.

    Family and domain databases

    Gene3Di 2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    HAMAPi MF_01201. Ala_racemase.
    InterProi IPR000821. 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 ]
    Pfami PF00842. Ala_racemase_C. 1 hit.
    PF01168. Ala_racemase_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00992. ALARACEMASE.
    SMARTi SM01005. Ala_racemase_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR00492. alr. 1 hit.
    PROSITEi PS00395. ALANINE_RACEMASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction."
      Tanizawa K., Ohshima A., Scheidegger A., Inagaki K., Tanaka H., Soda K.
      Biochemistry 27:1311-1316(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine."
      Faraci W.S., Walsh C.T.
      Biochemistry 28:431-437(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-43.
    3. "Time-dependent inhibition of Bacillus stearothermophilus alanine racemase by (1-aminoethyl)phosphonate isomers by isomerization to noncovalent slowly dissociating enzyme-(1-aminoethyl)phosphonate complexes."
      Badet B., Inagaki K., Soda K., Walsh C.T.
      Biochemistry 25:3275-3282(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-43.
    4. "Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase."
      Sun S., Toney M.D.
      Biochemistry 38:4058-4065(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-219.
    5. "Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine."
      Watanabe A., Yoshimura T., Mikami B., Esaki N.
      J. Biochem. 126:781-786(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACTIVE SITES, MUTAGENESIS.
    6. "Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance."
      Patrick W.M., Weisner J., Blackburn J.M.
      ChemBioChem 3:789-792(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-354.
    7. "Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution."
      Shaw J.P., Petsko G.A., Ringe D.
      Biochemistry 36:1329-1342(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-39, SEQUENCE REVISION.
    8. "Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine."
      Stamper C.G., Morollo A.A., Ringe D.
      Biochemistry 37:10438-10445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND L-ALA PHOSPHONATE, COFACTOR, ACTIVE SITE.
    9. "Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase."
      Morollo A.A., Petsko G.A., Ringe D.
      Biochemistry 38:3293-3301(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND PROPIONATE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-39, ENZYME REGULATION, CARBAMYLATION AT LYS-129.
      Strain: ATCC 12980 / DSM 22 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / VKM B-510.
    10. "Crystal stucture of alanine racemase in complex with D-alanine phosphonate."
      Stamper G.F., Ringe D.
      Submitted (SEP-2000) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH D-ALANINE PHOSPHONATE, CARBAMYLATION AT LYS-129.
    11. "Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine."
      Watanabe A., Yoshimura T., Mikami B., Hayashi H., Kagamiyama H., Esaki N.
      J. Biol. Chem. 277:19166-19172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE AND N-(5'-PHOSPHOPYRIDOXYL)-L-ALANINE, COFACTOR, ACTIVE SITE, PYRIDOXAL PHOSPHATE AT LYS-39, CARBAMYLATION AT LYS-129.
    12. "A side reaction of alanine racemase: transamination of cycloserine."
      Fenn T.D., Stamper G.F., Morollo A.A., Ringe D.
      Biochemistry 42:5775-5783(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND CYCLOSERINE, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, ACTIVE SITE, CARBAMYLATION AT LYS-129.
    13. "Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase."
      Fenn T.D., Holyoak T., Stamper G.F., Ringe D.
      Biochemistry 44:5317-5327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH CYCLOSERINE AND PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-39, MUTAGENESIS OF TYR-265, ENZYME REGULATION, ACTIVE SITE, CARBAMYLATION AT LYS-129.

    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: October 1, 2014
    This is version 117 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

    External Data

    Dasty 3