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Database: UniProt/SWISS-PROT
Entry: ALR_ACIBS
LinkDB: ALR_ACIBS
Original site: ALR_ACIBS 
ID   ALR_ACIBS               Reviewed;         367 AA.
AC   B0VNF6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   28-FEB-2018, entry version 62.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=ABSDF0117;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S.,
RA   Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S.,
RA   Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M.,
RA   Raoult D., Medigue C., Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CU468230; CAO99526.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0VNF6; -.
DR   SMR; B0VNF6; -.
DR   EnsemblBacteria; CAO99526; CAO99526; ABSDF0117.
DR   KEGG; abm:ABSDF0117; -.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    367       Alanine racemase.
FT                                /FTId=PRO_1000138577.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   367 AA;  40497 MW;  9EC41F7F73E52C85 CRC64;
     MPRPITAVIH RQALQNNLAV VRKAMPNSKV FAVVKANAYG HGIERVYEAF KAADGFALLD
     LEEAKRIRAL GWTGPILLLE GVFSPQDLFD CVQYQLSFTI HSEAQIEWVE QHPYPAQFDV
     FLKMNSGMSR LGFKPQHYVQ AWERLNNLAN VAKITHMMHF SDADGDRFGQ QGIDYQITAF
     EEIVKDLPGE RSVSNSAAIL RYQDQLKSDY VRSGIMLYGS SPDYPTHSIA DWGLQPTMSL
     RSEIISVQHL EPNESVGYGS NFVAEQPMTI GIVACGYADG YQRISPTGTP VLVDSVRTRT
     VGRVSMDMLA VDLTGIESAK VGSEVVLWGQ SSTGVVLPID DVAVSSGTVG YELMCAVTAR
     VQFINQV
//
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