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Database: UniProt
Entry: A1WUS2
LinkDB: A1WUS2
Original site: A1WUS2 
ID   ALR_HALHL               Reviewed;         364 AA.
AC   A1WUS2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JAN-2019, entry version 79.
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=Hhal_0652;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hoff W., Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:
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:0000255|HAMAP-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; CP000544; ABM61434.1; -; Genomic_DNA.
DR   RefSeq; WP_011813457.1; NC_008789.1.
DR   ProteinModelPortal; A1WUS2; -.
DR   SMR; A1WUS2; -.
DR   STRING; 349124.Hhal_0652; -.
DR   EnsemblBacteria; ABM61434; ABM61434; Hhal_0652.
DR   KEGG; hha:Hhal_0652; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000647; 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   Gene3D; 2.40.37.10; -; 1.
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    364       Alanine racemase.
FT                                /FTId=PRO_1000164599.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     304    304       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   364 AA;  38709 MW;  F2A57DA63AC7D9BC CRC64;
     MSRAARATVN LSALRANLRT ARAAAPQQRI MAVIKSDGYG HGLAVVAGAL TGHAEAFAVT
     DADEAEALRA AGFRERIVLL QGPFAVDDLA RAAAADLELV IHAHWQVEAL AQAQLASPVT
     VWLKVDSGMH RLGFPPEEVQ DAWRRLTEAS CVRADIGFLT HLACADDRDD PATERQLETF
     QAACDGLPGP RSAANSAGVL GWPASHYDWV RPGIMLYGAS PFVDGRDEQP ALQPAMAFQG
     RVVAVRHLRA GDPVGYGATW SCPEAMPVGV VSIGYGDGYP RHAPSGTPVE VAGQRTRLVG
     RISMDMLAVD LRGLDPVAEG DPAILWGGAV RAEEVAGACG TIAYELFCRM PPRVRREPVD
     GETL
//
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