ID   E3D1J2_NEIM7            Unreviewed;       352 AA.
AC   E3D1J2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=NMBB_1888 {ECO:0000313|EMBL:ADO32091.1};
OS   Neisseria meningitidis serogroup B (strain alpha710).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO32091.1, ECO:0000313|Proteomes:UP000006929};
RN   [1] {ECO:0000313|EMBL:ADO32091.1, ECO:0000313|Proteomes:UP000006929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX   PubMed=20709895; DOI=10.1128/JB.00883-10;
RA   Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA   Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT   "Comparative genome biology of a serogroup B carriage and disease strain
RT   supports a polygenic nature of meningococcal virulence.";
RL   J. Bacteriol. 192:5363-5377(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; CP001561; ADO32091.1; -; Genomic_DNA.
DR   RefSeq; WP_002218496.1; NC_017505.1.
DR   AlphaFoldDB; E3D1J2; -.
DR   KEGG; nmp:NMBB_1888; -.
DR   PATRIC; fig|630588.3.peg.2178; -.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006929; 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          229..351
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        250
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   352 AA;  38802 MW;  C0EEFE13486F2756 CRC64;
     MRPLNVQIRL GNLRHNYRIL KEMHGGKLLA VVKADAYGHG AVRCAFALAD LADGFAVATI
     DEGIRLRESG ITHPIVLLEG VFEASEYEAV EQYSLWPAVG NQWQLEALLS RHWKKPVKVW
     LKMDSGMHRT GFFPHDYASA YAALKQSEYV DSIVKFSHFS CADEPESGIT EIQMEAFDLG
     TEGLEGEESL ANSAAILNVP EARRDWGRAG LALYGISPFG GSDDRLKPVM RLSTRIFGER
     VLQPHSPIGY GATFYTSKST RVGLIACGYA DGYPRRAPSN SPVAVDGKLT RVIGRVSMDM
     MTIELDASQE GLGHEVELWG DTVNINTVAE AAGTIPYELM CNIKRAKFTY IE
//