ID   A0A1I9XVD5_9BURK        Unreviewed;       363 AA.
AC   A0A1I9XVD5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=YQ44_07585 {ECO:0000313|EMBL:APA67727.1};
OS   Janthinobacterium sp. 1_2014MBL_MicDiv.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1644131 {ECO:0000313|EMBL:APA67727.1, ECO:0000313|Proteomes:UP000180140};
RN   [1] {ECO:0000313|EMBL:APA67727.1, ECO:0000313|Proteomes:UP000180140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_2014MBL_MicDiv {ECO:0000313|EMBL:APA67727.1,
RC   ECO:0000313|Proteomes:UP000180140};
RA   Roller B., Bhatnagar S., Boitano M., Korlach J., Newman D.K.,
RA   Leadbetter J.R., Dawson S.C.;
RT   "The Complete Genome Sequence of Janthinobacterium sp. str.
RT   1_2014MBL_MicDiv.";
RL   Submitted (APR-2015) 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,
CC         ECO:0000256|HAMAP-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; CP011319; APA67727.1; -; Genomic_DNA.
DR   RefSeq; WP_071322856.1; NZ_CP011319.1.
DR   AlphaFoldDB; A0A1I9XVD5; -.
DR   STRING; 1644131.YQ44_07585; -.
DR   KEGG; jaz:YQ44_07585; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000180140; 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; cd06827; PLPDE_III_AR_proteobact; 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          239..363
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        260
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   363 AA;  38317 MW;  70BE11B2315E88B9 CRC64;
     MPRPLIATIH LDAMQHNLAR ARACAQGAKV WAVVKANAYG HGLERAMRGF AHADGLALVE
     VDYAVRLREL GWTKPILLLE GFFDASDLPV MAQYGLSGSV HCVEQIAMLE AARLPRPIDV
     QLKMNTGMNR LGFTPQAVAA AYARLRAMPH VGTITLMTHF ANADEAAPTR MPLAQQMLRF
     EAGAASIGTP LPRSLCNSAG LLLHRLDSDW VRPGIMLYGG TPSGAPGGTS AQAFGLLPTM
     TLRSSIIGIQ DIAAGEVVGY GSRYEAAGNV KVGVVACGYA DGYPRHAPEG TPVLVDGVRT
     VLIGRVSMDM LMVDLTPVPG ARVGSSVTLW GQGMPIDEVA LAAGTIGYEL MCALAPRVPV
     TEG
//