ID   D5H6C9_SALRM            Unreviewed;       465 AA.
AC   D5H6C9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
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:CBH23584.1};
GN   OrderedLocusNames=SRM_00663 {ECO:0000313|EMBL:CBH23584.1};
OS   Salinibacter ruber (strain M8).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23584.1, ECO:0000313|Proteomes:UP000000933};
RN   [1] {ECO:0000313|EMBL:CBH23584.1, ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|EMBL:CBH23584.1,
RC   ECO:0000313|Proteomes:UP000000933};
RX   PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA   Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA   Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA   Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA   Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT   "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT   in two coexisting Salinibacter ruber strains.";
RL   ISME J. 4:882-895(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG   Genoscope;
RT   "Genome sequence of Salinibacter ruber M8.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; FP565814; CBH23584.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5H6C9; -.
DR   KEGG; srm:SRM_00663; -.
DR   PATRIC; fig|761659.10.peg.743; -.
DR   HOGENOM; CLU_028393_1_1_10; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000933; 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          305..435
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   REGION          435..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        99
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        326
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   465 AA;  48585 MW;  3A63DD4326E1328B CRC64;
     MPVDSTGRGP VGCEAGGRGE HVRRAIGAGS FGNHRPGRRL SCACSLIFAR SPVPFAIDRS
     PHTVGAAPVT ATVDLAAIQH NAGVLQERAG GADVMAIIKA DAYGHGVRPV ARAAYEAGIR
     HYGVARLPEG VHLREAGHGG RILVLGAPAP TQLPRYAEYD LDLTVPSADI AAAVVRHASP
     EAPLRVHVTV DTGMGRLGLA PDDVPAVMTR LADAPGVRLA GLWTHFATAD APGSSFAQTQ
     LDRFRAVVDA VDVDVEHVHA ANTGGLLTIG APTHEFDASL VRSGIALYGL AATPELSARL
     DLRPAMRLAA RVTHLKTVPA GTPISYGAQW EAPRRTRIAT LGIGYGDGYP RRCSGRASVR
     IGGASCPIVG TICMDMCMVD LGPPNEAPAT RVDRGDEAVL FGPAGPTAYD VAQWSDTIPY
     EILCGVSPRV PRRHVNCTDE NGTDENGTDD MRAPSRLTRP TASGG
//