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Database: UniProt
Entry: Q5HED1
LinkDB: Q5HED1
Original site: Q5HED1 
ID   ALR1_STAAC              Reviewed;         382 AA.
AC   Q5HED1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 92.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; Synonyms=alr; OrderedLocusNames=SACOL2060;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS), AND SUBUNIT.
RG   Center for structural genomics of infectious diseases (CSGID);
RT   "2.37 Angstrom resolution crystal structure of an alanine racemase
RT   (alr) from Staphylococcus aureus subsp. aureus COL.";
RL   Submitted (AUG-2010) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000046; AAW37022.1; -; Genomic_DNA.
DR   RefSeq; WP_001281145.1; NC_002951.2.
DR   PDB; 3OO2; X-ray; 2.37 A; A/B=1-382.
DR   PDBsum; 3OO2; -.
DR   ProteinModelPortal; Q5HED1; -.
DR   SMR; Q5HED1; -.
DR   STRING; 93062.SACOL2060; -.
DR   EnsemblBacteria; AAW37022; AAW37022; SACOL2060.
DR   KEGG; sac:SACOL2060; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   BioCyc; SAUR93062:G1G4B-2267-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   EvolutionaryTrace; Q5HED1; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    382       Alanine racemase 1.
FT                                /FTId=PRO_0000114567.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   STRAND        7     14       {ECO:0000244|PDB:3OO2}.
FT   HELIX        15     28       {ECO:0000244|PDB:3OO2}.
FT   STRAND       32     37       {ECO:0000244|PDB:3OO2}.
FT   HELIX        39     43       {ECO:0000244|PDB:3OO2}.
FT   HELIX        47     56       {ECO:0000244|PDB:3OO2}.
FT   STRAND       61     66       {ECO:0000244|PDB:3OO2}.
FT   HELIX        67     74       {ECO:0000244|PDB:3OO2}.
FT   TURN         75     77       {ECO:0000244|PDB:3OO2}.
FT   STRAND       80     84       {ECO:0000244|PDB:3OO2}.
FT   HELIX        90     92       {ECO:0000244|PDB:3OO2}.
FT   HELIX        93     98       {ECO:0000244|PDB:3OO2}.
FT   STRAND      101    105       {ECO:0000244|PDB:3OO2}.
FT   HELIX       108    116       {ECO:0000244|PDB:3OO2}.
FT   STRAND      126    132       {ECO:0000244|PDB:3OO2}.
FT   STRAND      139    141       {ECO:0000244|PDB:3OO2}.
FT   HELIX       144    154       {ECO:0000244|PDB:3OO2}.
FT   STRAND      160    166       {ECO:0000244|PDB:3OO2}.
FT   STRAND      174    177       {ECO:0000244|PDB:3OO2}.
FT   HELIX       178    191       {ECO:0000244|PDB:3OO2}.
FT   STRAND      197    202       {ECO:0000244|PDB:3OO2}.
FT   HELIX       204    209       {ECO:0000244|PDB:3OO2}.
FT   HELIX       222    225       {ECO:0000244|PDB:3OO2}.
FT   HELIX       231    236       {ECO:0000244|PDB:3OO2}.
FT   STRAND      245    250       {ECO:0000244|PDB:3OO2}.
FT   STRAND      253    257       {ECO:0000244|PDB:3OO2}.
FT   STRAND      275    281       {ECO:0000244|PDB:3OO2}.
FT   HELIX       284    286       {ECO:0000244|PDB:3OO2}.
FT   HELIX       290    292       {ECO:0000244|PDB:3OO2}.
FT   STRAND      296    299       {ECO:0000244|PDB:3OO2}.
FT   STRAND      302    308       {ECO:0000244|PDB:3OO2}.
FT   STRAND      315    319       {ECO:0000244|PDB:3OO2}.
FT   STRAND      328    332       {ECO:0000244|PDB:3OO2}.
FT   STRAND      336    338       {ECO:0000244|PDB:3OO2}.
FT   HELIX       342    348       {ECO:0000244|PDB:3OO2}.
FT   HELIX       353    359       {ECO:0000244|PDB:3OO2}.
FT   STRAND      366    370       {ECO:0000244|PDB:3OO2}.
FT   STRAND      373    377       {ECO:0000244|PDB:3OO2}.
FT   HELIX       379    381       {ECO:0000244|PDB:3OO2}.
SQ   SEQUENCE   382 AA;  42823 MW;  52B3C88E9811956D CRC64;
     MSDKYYRSAY MNVDLNAVAS NFKVFSTLHP NKTVMAVVKA NAYGLGSVKV ARHLMENGAT
     FFAVATLDEA IELRMHGITA KILVLGVLPA KDIDKAIQHR VALTVPSKQW LKEAIKNISG
     EQEKKLWLHI KLDTGMGRLG IKDTKTYQEV IEIIQQYEQL VFEGVFTHFA CADEPGDMTT
     EQYQRFKDMV NEAIKPEYIH CQNSAGSLLM DCQFCNAIRP GISLYGYYPS EYVQQKVKVH
     LKPSVQLIAN VVQTKTLQAG ESVSYGATYT ATDPTTIALL PIGYADGYLR IMQGSFVNVN
     GHQCEVIGRV CMDQTIVKVP DQVKAGDSVI LIDNHRESPQ SVEVVAEKQH TINYEVLCNL
     SRRLPRIYHD GDQRFVTNEL LK
//
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