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Database: UniProt
Entry: P63479
LinkDB: P63479
Original site: P63479 
ID   ALR1_STAAM              Reviewed;         382 AA.
AC   P63479; Q99SI5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 96.
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=SAV2070;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE AND ACETATE, CATALYTIC ACTIVITY, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, ACTIVE SITE,
RP   PYRIDOXAL PHOSPHATE AT LYS-39, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=22194336; DOI=10.1107/S0907444911050682;
RA   Scaletti E.R., Luckner S.R., Krause K.L.;
RT   "Structural features and kinetic characterization of alanine racemase
RT   from Staphylococcus aureus (Mu50).";
RL   Acta Crystallogr. D 68:82-92(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. {ECO:0000269|PubMed:22194336}.
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         ECO:0000269|PubMed:22194336};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201,
CC         ECO:0000269|PubMed:22194336};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.89 mM for D-alanine (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:22194336};
CC         KM=2.77 mM for L-alanine (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:22194336};
CC         Vmax=91 umol/min/mg enzyme toward D-alanine (at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:22194336};
CC         Vmax=250 umol/min/mg enzyme toward L-alanine (at 30 degrees
CC         Celsius) {ECO:0000269|PubMed:22194336};
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:0000269|PubMed:22194336}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; BA000017; BAB58232.1; -; Genomic_DNA.
DR   RefSeq; WP_001281154.1; NC_002758.2.
DR   PDB; 4A3Q; X-ray; 2.15 A; A/B=1-382.
DR   PDB; 6G56; X-ray; 2.15 A; A/B=2-382.
DR   PDB; 6G58; X-ray; 1.90 A; A/B=2-382.
DR   PDB; 6G59; X-ray; 2.45 A; A/B=2-382.
DR   PDBsum; 4A3Q; -.
DR   PDBsum; 6G56; -.
DR   PDBsum; 6G58; -.
DR   PDBsum; 6G59; -.
DR   ProteinModelPortal; P63479; -.
DR   SMR; P63479; -.
DR   STRING; 158878.SAV2070; -.
DR   World-2DPAGE; 0002:P63479; -.
DR   PaxDb; P63479; -.
DR   EnsemblBacteria; BAB58232; BAB58232; SAV2070.
DR   KEGG; sav:SAV2070; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   PhylomeDB; P63479; -.
DR   BioCyc; SAUR158878:SAV_RS11330-MONOMER; -.
DR   BRENDA; 5.1.1.1; 3352.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002481; 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_0000114568.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000305|PubMed:22194336}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000305|PubMed:22194336}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000305}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT   STRAND        7     14       {ECO:0000244|PDB:6G58}.
FT   HELIX        15     28       {ECO:0000244|PDB:6G58}.
FT   STRAND       32     34       {ECO:0000244|PDB:6G58}.
FT   HELIX        39     43       {ECO:0000244|PDB:6G58}.
FT   HELIX        47     56       {ECO:0000244|PDB:6G58}.
FT   STRAND       61     66       {ECO:0000244|PDB:6G58}.
FT   HELIX        67     75       {ECO:0000244|PDB:6G58}.
FT   STRAND       80     84       {ECO:0000244|PDB:6G58}.
FT   HELIX        90     92       {ECO:0000244|PDB:6G58}.
FT   HELIX        93     98       {ECO:0000244|PDB:6G58}.
FT   STRAND      102    105       {ECO:0000244|PDB:6G58}.
FT   HELIX       108    116       {ECO:0000244|PDB:6G58}.
FT   STRAND      126    132       {ECO:0000244|PDB:6G58}.
FT   STRAND      134    136       {ECO:0000244|PDB:6G58}.
FT   STRAND      138    141       {ECO:0000244|PDB:6G58}.
FT   HELIX       144    155       {ECO:0000244|PDB:6G58}.
FT   STRAND      160    166       {ECO:0000244|PDB:6G58}.
FT   STRAND      174    177       {ECO:0000244|PDB:6G58}.
FT   HELIX       178    190       {ECO:0000244|PDB:6G58}.
FT   STRAND      197    200       {ECO:0000244|PDB:6G58}.
FT   HELIX       204    209       {ECO:0000244|PDB:6G58}.
FT   STRAND      216    218       {ECO:0000244|PDB:6G58}.
FT   HELIX       222    225       {ECO:0000244|PDB:6G58}.
FT   HELIX       231    236       {ECO:0000244|PDB:6G58}.
FT   STRAND      245    250       {ECO:0000244|PDB:6G58}.
FT   STRAND      253    257       {ECO:0000244|PDB:6G58}.
FT   STRAND      262    264       {ECO:0000244|PDB:6G59}.
FT   HELIX       265    267       {ECO:0000244|PDB:6G58}.
FT   STRAND      275    281       {ECO:0000244|PDB:6G58}.
FT   HELIX       284    286       {ECO:0000244|PDB:6G58}.
FT   HELIX       290    292       {ECO:0000244|PDB:6G58}.
FT   STRAND      296    299       {ECO:0000244|PDB:6G58}.
FT   STRAND      302    306       {ECO:0000244|PDB:6G58}.
FT   STRAND      315    318       {ECO:0000244|PDB:6G58}.
FT   STRAND      328    332       {ECO:0000244|PDB:6G58}.
FT   STRAND      336    338       {ECO:0000244|PDB:6G58}.
FT   HELIX       342    348       {ECO:0000244|PDB:6G58}.
FT   HELIX       353    358       {ECO:0000244|PDB:6G58}.
FT   STRAND      366    370       {ECO:0000244|PDB:6G58}.
FT   STRAND      373    377       {ECO:0000244|PDB:6G58}.
FT   HELIX       379    381       {ECO:0000244|PDB:6G58}.
SQ   SEQUENCE   382 AA;  42809 MW;  A46B7E55F5A65E41 CRC64;
     MSDKYYRSAY MNVDLNAVAS NFKVFSTLHP NKTVMAVVKA NAYGLGSVKV ARHLMENGAT
     FFAVATLDEA IELRMHGITA KILVLGVLPA KDIDKAIQHR VALTVPSKQW LKEAIKNISG
     EQEKKLWLHI KLDTGMGRLG IKDTNTYQEV 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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