ID   E6NSA8_HELPQ            Unreviewed;       377 AA.
AC   E6NSA8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:BAJ60024.1};
GN   OrderedLocusNames=HPF57_0950 {ECO:0000313|EMBL:BAJ60024.1};
OS   Helicobacter pylori (strain F57).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ60024.1, ECO:0000313|Proteomes:UP000008082};
RN   [1] {ECO:0000313|EMBL:BAJ60024.1, ECO:0000313|Proteomes:UP000008082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F57 {ECO:0000313|EMBL:BAJ60024.1,
RC   ECO:0000313|Proteomes:UP000008082};
RX   PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA   Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA   Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT   "Evolution in an oncogenic bacterial species with extreme genome
RT   plasticity: Helicobacter pylori East Asian genomes.";
RL   BMC Microbiol. 11:104-104(2011).
RN   [2] {ECO:0000313|EMBL:BAJ60024.1, ECO:0000313|Proteomes:UP000008082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F57 {ECO:0000313|EMBL:BAJ60024.1,
RC   ECO:0000313|Proteomes:UP000008082};
RX   PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA   Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA   Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT   "Birth and death of genes linked to chromosomal inversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; AP011945; BAJ60024.1; -; Genomic_DNA.
DR   RefSeq; WP_000917947.1; NC_017367.1.
DR   AlphaFoldDB; E6NSA8; -.
DR   KEGG; hex:HPF57_0950; -.
DR   PATRIC; fig|866346.4.peg.1014; -.
DR   HOGENOM; CLU_028393_2_2_7; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008082; 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   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          250..377
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        37
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        271
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         37
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   377 AA;  41825 MW;  E4DE998F44A3919A CRC64;
     MLKRASFVEV NSSSLRHNFS AVKSIVPKDA HIMAVVKANA YGAGAIKASE IFLQEGANYL
     GVATLDEALE LRSHFSKTPI LILGYSPNAN ASMLIDNDLS AMIFSLEQAE VFSQMALKSQ
     KRLKIHLKID TGMHRLGLEP NFKSIEIIKK IRALKGLEIE GIFTHLSNAD SNIKTHAKNQ
     MKAFNAFLEQ LLNQKIEFQY RHAYNSAGIL SLCNGNENRF LNLYRPGIML YGFYPSNGMK
     ETCPTILKNV ISLKAQIVQI RSVKKGEFIG YGEHFYTNEE TLVGVLALGY ADGLMRALGN
     RIQVAINNQL APLIGKVCMD QCFVKLNNIQ AKEGDEAILF GDKSAKANDA SEIAALLNTI
     PYETISTLSK RLERVYI
//