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Database: UniProt
Entry: Q9S5V6
LinkDB: Q9S5V6
Original site: Q9S5V6 
ID   ALR_BACPS               Reviewed;         383 AA.
AC   Q9S5V6; O82941;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 88.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr;
OS   Bacillus psychrosaccharolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RX   PubMed=10080917; DOI=10.1006/bbrc.1999.0324;
RA   Okubo Y., Yokoigawa K., Esaki N., Soda K., Kawai H.;
RT   "Characterization of psychrophilic alanine racemase from Bacillus
RT   psychrosaccharolyticus.";
RL   Biochem. Biophys. Res. Commun. 256:333-340(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-166.
RA   Okubo Y., Yokoigawa K., Kawai H.;
RT   "Alanine racemase gene fragments as probes for detecting Bacillus
RT   stearothermophilus and Bacillus psychrosaccharolyticus in foods.";
RL   J. Ferment. Bioeng. 85:559-563(1998).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Does not act on other amino acids.
CC       {ECO:0000269|PubMed:10080917}.
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:10080917};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201,
CC         ECO:0000269|PubMed:10080917};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for pyridoxal phosphate {ECO:0000269|PubMed:10080917};
CC         KM=12.2 mM for D-alanine {ECO:0000269|PubMed:10080917};
CC         KM=17.9 mM for L-alanine {ECO:0000269|PubMed:10080917};
CC       pH dependence:
CC         Optimum pH is 8-10. {ECO:0000269|PubMed:10080917};
CC       Temperature dependence:
CC         Highly active at low temperatures, even at 0 degree Celsius.
CC         Thermolabile. {ECO:0000269|PubMed:10080917};
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:10080917}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AB021683; BAA76373.1; -; Genomic_DNA.
DR   EMBL; AB011668; BAA31255.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9S5V6; -.
DR   SMR; Q9S5V6; -.
DR   PRIDE; Q9S5V6; -.
DR   BRENDA; 5.1.1.1; 7181.
DR   UniPathway; UPA00042; UER00497.
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   Direct protein sequencing; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    383       Alanine racemase.
FT                                /FTId=PRO_0000114498.
FT   ACT_SITE     41     41       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    266    266       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     313    313       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   383 AA;  42519 MW;  E6DE9421EEFC5BF7 CRC64;
     MTLQNFYRDT WAEINLDAIF ENAANMKKHL PPEITLFAVV KANAYGHGDV EVAETAIQAG
     AGYLAVAFLD EALALRKKGI TAPILVLGAS RPEDAQIAAR ESITLTVFQA GWLEAAQSFL
     EGTVLTIHLK CDSGMGRIGI RKQEEMNEIE RFLQKTKCFV LEGIFTHFAT ADQLDTEYFS
     KQLARFEEML TWLKEKPKYV HAANSAALLR FPNAVFNSVR MGISLYGLSP SMEMKEVLPF
     ALRPAFSLKT KLVHVKNISK GQSVSYGATY TAEEDTWIGT LPIGYADGWI RMLQGQEVLL
     EGGRSPLVGR ICMDQCMVKL SREFPVGTEV TLIGKNGTEC ITVDDIAEKL NTINYEVTCM
     ISSRVPRMYL KDGRITGVVN QLI
//
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