ID   E5AUN4_MYCRK            Unreviewed;       356 AA.
AC   E5AUN4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=RBRH_00324 {ECO:0000313|EMBL:CBW76808.1};
OS   Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
OS   (Paraburkholderia rhizoxinica).
OG   Plasmid pBRH01 {ECO:0000313|EMBL:CBW76808.1,
OG   ECO:0000313|Proteomes:UP000007437}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Mycetohabitans.
OX   NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW76808.1, ECO:0000313|Proteomes:UP000007437};
RN   [1] {ECO:0000313|EMBL:CBW76808.1, ECO:0000313|Proteomes:UP000007437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19002 / CIP 109453 / HKI 454
RC   {ECO:0000313|Proteomes:UP000007437};
RC   PLASMID=pBRH01 {ECO:0000313|EMBL:CBW76808.1,
RC   ECO:0000313|Proteomes:UP000007437};
RX   PubMed=21131495; DOI=10.1128/JB.01318-10;
RA   Lackner G., Moebius N., Partida-Martinez L., Hertweck C.;
RT   "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont of
RT   Rhizopus microsporus.";
RL   J. Bacteriol. 193:783-784(2011).
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; FR687360; CBW76808.1; -; Genomic_DNA.
DR   RefSeq; WP_013428669.1; NC_014718.1.
DR   AlphaFoldDB; E5AUN4; -.
DR   KEGG; brh:RBRH_00324; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007437; Plasmid pBRH01.
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   Plasmid {ECO:0000313|EMBL:CBW76808.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          232..356
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        253
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         301
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   356 AA;  38159 MW;  4D2934A807762B66 CRC64;
     MPRPLLATIH TAALANNLAV ARRHASKSKL WAVVKANAYG HGLARVFPGL RSTDGFGLLD
     LEEAVKLREL GWAGPILLLE GFFRPTDIDV IDRYSLTTTV HCDEQLRMLE MARLSKPVNI
     QLKMNSGMNR LGYVAGKYRA AWERARACPS VGQITLMTHF SDADGEMGIR HQLEVFEHGA
     EGIAGSRSLA NSAATLWHPY AHFDWVRPGI ILYGASPSGV SAAIEGLGLQ PAMTLSSELI
     AVQTVEPGDS VGYGSAFKAR ERMRIGVVAC GYADGYPRCA PEGTPVQVGG VRTRVVGRVS
     MDMLTVDLSS CPNAVIGSPV QLWGADVPID DVAAACGTVG YELMCAVAQR VSVRAE
//