ID   H9ZTH0_THETH            Unreviewed;       360 AA.
AC   H9ZTH0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=TtJL18_1761 {ECO:0000313|EMBL:AFH39630.1};
OS   Thermus thermophilus JL-18.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH39630.1, ECO:0000313|Proteomes:UP000007388};
RN   [1] {ECO:0000313|EMBL:AFH39630.1, ECO:0000313|Proteomes:UP000007388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL-18 {ECO:0000313|EMBL:AFH39630.1,
RC   ECO:0000313|Proteomes:UP000007388};
RX   PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA   Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA   Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA   Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA   Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA   Hedlund B.P.;
RT   "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT   JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL   Genome Announc. 1:E00106-E00112(2013).
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; CP003252; AFH39630.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9ZTH0; -.
DR   STRING; 798128.TtJL18_1761; -.
DR   KEGG; ttl:TtJL18_1761; -.
DR   PATRIC; fig|798128.4.peg.1706; -.
DR   HOGENOM; CLU_028393_2_1_0; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007388; 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          235..359
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        43
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        256
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         43
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   360 AA;  38856 MW;  1122843A02FEF2DF CRC64;
     MRPRGYPKGV QARAWIEVDL AALWANYRLL AGRAGGEVIP VLKADAYGHG ALPLARFLEG
     KGVGRFAVAT LEEGRRLREG GIKGEVLLLG SLHPLEAEEA LELGLVPTLS TLEAAEALSL
     RARALGLVPR AHLKVDTGMN RVGFPWEEAA SALRAVEAMG VRVEGVYTHL ATAGEDAAFV
     ETQRRRFQEV RRALGENYFY HLENSLGLLR HGATAGVRVG LALYGLVPGF GLRPILRILA
     RPTLVKRLKA GDRVGYGGVY VARGGEWLAT LPVGYADGLP WGAVRFVKGP DGRLLEVAGR
     ISMDQTTVLL PGPVGLEAVF EVLSADFGPT GLLAWAEARG TLPYEVAVHL SRRLPRRYLE
//