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Database: UniProt/SWISS-PROT
Entry: ALR_HELPS
LinkDB: ALR_HELPS
Original site: ALR_HELPS 
ID   ALR_HELPS               Reviewed;         377 AA.
AC   B2UU89;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   05-DEC-2018, entry version 65.
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; OrderedLocusNames=HPSH_04955;
OS   Helicobacter pylori (strain Shi470).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=512562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shi470;
RA   Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT   "Genome sequence of Helicobacter pylori from the remote Amazon: traces
RT   of Asian ancestry of the first Americans.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001072; ACD48421.1; -; Genomic_DNA.
DR   RefSeq; WP_000918001.1; NC_010698.2.
DR   ProteinModelPortal; B2UU89; -.
DR   SMR; B2UU89; -.
DR   EnsemblBacteria; ACD48421; ACD48421; HPSH_04955.
DR   KEGG; hps:HPSH_04955; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; HPYL512562:G1GBY-952-MONOMER; -.
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; 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.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    377       Alanine racemase.
FT                                /FTId=PRO_1000138603.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     319    319       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   377 AA;  41812 MW;  C82D7CD4EB9E55FD CRC64;
     MLKRASFVEV NTASLRHNFS AVKSIVPKDA HIMAVVKANA YGVGAIKASE IFLQEGAHYL
     GVATLDEALE LHSHFSKTPI LILGYSPNSN ASMLIDNDLS AMIFSLEQAE VFSQTALKSQ
     KRLKVHLKID TGMHRLGLEP NFKSIEIIKK IRALKGLEVE GIFTHLSNAD AKIKTHAKNQ
     MKAFNAFLEQ LSNQKIEFQY RHAYNSAGIL SLCNGNENRF LNLYRPGIML YGFYPSNGMK
     ETCPTILKNV ISLKAQIVQI RSVKKGEFIG YGEHFYTNEE TLVGVLALGY ADGLMRALGN
     RIQVAINNQL APLIGKVCMD QCFVKLNNIQ AKEGDEVILF GDKSAKANDA SEIAALLNTI
     PYETISTLSK RLERVYI
//
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