GenomeNet

Database: UniProt
Entry: P63482
LinkDB: P63482
Original site: P63482 
ID   ALR2_STAAM              Reviewed;         361 AA.
AC   P63482; Q99U86;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 87.
DE   RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr2; OrderedLocusNames=SAV1399;
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).
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   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; BA000017; BAB57561.1; -; Genomic_DNA.
DR   RefSeq; WP_000127595.1; NC_002758.2.
DR   ProteinModelPortal; P63482; -.
DR   STRING; 158878.SAV1399; -.
DR   World-2DPAGE; 0002:P63482; -.
DR   PaxDb; P63482; -.
DR   PRIDE; P63482; -.
DR   EnsemblBacteria; BAB57561; BAB57561; SAV1399.
DR   KEGG; sav:SAV1399; -.
DR   eggNOG; ENOG4108XFP; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000280025; -.
DR   KO; K01775; -.
DR   OMA; VHLEYEN; -.
DR   PhylomeDB; P63482; -.
DR   BioCyc; SAUR158878:SAV_RS07535-MONOMER; -.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    361       Alanine racemase 2.
FT                                /FTId=PRO_0000114577.
FT   ACT_SITE     30     30       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     122    122       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      30     30       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   361 AA;  41396 MW;  1EA4213C509CF5CA CRC64;
     MTATWSVNKK IFLQNAITVK NNQPLMAVVK NNAYHYDLEF AVTQFIHAGI DTFSTTSLRE
     AIQIRQLAPD ATIFLMNAVY EFDLVREHQI HMTLPSLTYY YNHKNDLAGI HVHLEFENLL
     HRSGFKDLNE IKEVLKDHHH NQNAKMIISG LWTHFGYADE FDVSDYNVER SQWMEIVEAL
     LSEGYQFDLI HAQNSASFYR EGQILLPHHT HARVGIALYG SRPYSSLNQH DIVQSLTVKA
     HVIQVREVQA GDYCGYSFAF EVTKNNTKLA VVDIGYGDGI LRTRAKHEAL INGKRYPIRA
     LMMSHMFVEV DGNVHAQDEV ILYNNDIRID EYTFKGVGAN SEQLSAMNHD SLKKEYISND
     C
//
DBGET integrated database retrieval system