ID   D7B7P7_NOCDD            Unreviewed;       376 AA.
AC   D7B7P7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=Ndas_4045 {ECO:0000313|EMBL:ADH69442.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH69442.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH69442.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(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; CP002040; ADH69442.1; -; Genomic_DNA.
DR   RefSeq; WP_013155049.1; NC_014210.1.
DR   AlphaFoldDB; D7B7P7; -.
DR   STRING; 446468.Ndas_4045; -.
DR   KEGG; nda:Ndas_4045; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_0_0_11; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002219; Chromosome 1.
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:UP000002219}.
FT   DOMAIN          243..372
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        264
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         312
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   376 AA;  39531 MW;  41F76288EB34F862 CRC64;
     MSHFAHARVD LDAISHNARV LRGFAGGTPL MGVVKADGYG HGMLPAARAL IAGGATWLGT
     AFIGEALELR RAGLTPPVLA WIIPPGEPVA EAVEADIDLG VSDRAVLDTV IAEARRIGRT
     ARVQLKADTG LNRGGVGPAD WGALAEAAAR AEDEGHLRVT GVWSHFACAD EPGHPSVARQ
     LSRFHEALET ADKVGLTPEV RHIANSAALL TLPEARFDLV RGGIASYGLS PIPGLTGTGL
     RPAMTLRSRL ALTKRVPEGS GVSYGHRYVT DRETTLALVP LGYADGVPRA ATNRGPVLLG
     GRRRAVAGTV CMDQFVVDVG DDAVEAGEYA VLFGNPEDHP DTPTAEDWAE ILDTIPYEIV
     TRVGPRVPRE YVGGGA
//