ID   C7BYY8_HELPB            Unreviewed;       377 AA.
AC   C7BYY8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:CAX29451.1};
GN   OrderedLocusNames=HELPY_0927 {ECO:0000313|EMBL:CAX29451.1};
OS   Helicobacter pylori (strain B38).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=592205 {ECO:0000313|EMBL:CAX29451.1, ECO:0000313|Proteomes:UP000000313};
RN   [1] {ECO:0000313|EMBL:CAX29451.1, ECO:0000313|Proteomes:UP000000313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B38 {ECO:0000313|EMBL:CAX29451.1,
RC   ECO:0000313|Proteomes:UP000000313};
RX   PubMed=20537153; DOI=10.1186/1471-2164-11-368;
RA   Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S.,
RA   Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C., Ruskone-Foumestraux A.,
RA   Courillon-Mallet A., De Reuse H., Boneca I.G., Lamarque D., Megraud F.,
RA   Delchier J.C., Medigue C., Bouchier C., Labigne A., Raymond J.;
RT   "From array-based hybridization of Helicobacter pylori isolates to the
RT   complete genome sequence of an isolate associated with MALT lymphoma.";
RL   BMC Genomics 11:368-368(2010).
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; FM991728; CAX29451.1; -; Genomic_DNA.
DR   RefSeq; WP_000917905.1; NC_012973.1.
DR   AlphaFoldDB; C7BYY8; -.
DR   KEGG; hpb:HELPY_0927; -.
DR   HOGENOM; CLU_028393_2_2_7; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000313; 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; 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.
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;  41920 MW;  C9C7127EE08697D6 CRC64;
     MLKRASFVEV DTASLRHNFS AVKSIIPKDA CVMAVVKANA YGVGAIKASE IFLQEGANYL
     GVAALDEALE LRSYFSKTPI LILGYSPNSN ASMLIDNDLS AMVFSFEQAE VFSQMALKSQ
     KRLKVHLKID TGMHRLGLEP NFKSIEIIKK IRALKGLEVE GIFTHLSNAD AKIKTHAKNQ
     MKAFNAFLEQ LLDQKIEFQY RHAYNSAGIL SLCNGNENRF LNLYRPGIML YGFYPSNEMK
     ESCPTILKNV VSLKAQIVQI RSVKKGEFIG YGEHFYTNEE TLVGVLALGY ADGLVRALGN
     RIQVAINNQL APLIGKVCMD QCFVKLNDIQ AKEGDEVILF GDKSTKANDA SEIAVLLNTI
     PYETISTLSK RLERVYI
//