ID   D3PDB4_DEFDS            Unreviewed;       363 AA.
AC   D3PDB4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 85.
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:BAI80587.1};
GN   OrderedLocusNames=DEFDS_1118 {ECO:0000313|EMBL:BAI80587.1};
OS   Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS   SSM1).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Deferribacteraceae; Deferribacter.
OX   NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI80587.1, ECO:0000313|Proteomes:UP000001520};
RN   [1] {ECO:0000313|EMBL:BAI80587.1, ECO:0000313|Proteomes:UP000001520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC   {ECO:0000313|Proteomes:UP000001520};
RX   PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA   Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA   Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA   Takai K.;
RT   "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT   the genome sequence of the thermophilic bacterium Deferribacter
RT   desulfuricans SSM1.";
RL   DNA Res. 17:123-137(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; AP011529; BAI80587.1; -; Genomic_DNA.
DR   RefSeq; WP_013007834.1; NC_013939.1.
DR   AlphaFoldDB; D3PDB4; -.
DR   STRING; 639282.DEFDS_1118; -.
DR   KEGG; ddf:DEFDS_1118; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_0; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001520; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001520}.
FT   DOMAIN          237..361
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        258
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   363 AA;  41130 MW;  98B483768899684C CRC64;
     MLTKIKTLRP TYAEINLANY KHNIEVAKSL SKSKIIAIVK ADAYGHGAIK LSKFAYEQCD
     VKDFGVATIE EGVNLRNVLP TDARIITLGY IDEHHFEELL HHKITPTVFD KSIMAKLDKF
     AKGNNVVLDV VLKIDTGMNR LGFGLNTDFN ELVESYSNLN IVLMMTHLSS SDTDLDYTKW
     QINRFDEYLK RYNVKAETSV FNSSAICFYS NKYTYTRPGI MSYGYVYPEN RFGLKPVMSI
     YSKLIHIKRL KKGEKISYNQ TFTASKDMKI GVIPIGYADG YFRALSNKGV MFVNGKPCNV
     VGTVCMDMTM IDITHLNESD LDCEVEVLGK HIDAEQIAKM CNTISYEIVC AISDRIPRVY
     INA
//