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Database: UniProt/TrEMBL
Entry: H6NSY9_9BACL
LinkDB: H6NSY9_9BACL
Original site: H6NSY9_9BACL 
ID   H6NSY9_9BACL            Unreviewed;       394 AA.
AC   H6NSY9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-SEP-2017, entry version 43.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=PM3016_563 {ECO:0000313|EMBL:AFC27530.1};
OS   Paenibacillus mucilaginosus 3016.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC27530.1, ECO:0000313|Proteomes:UP000007523};
RN   [1] {ECO:0000313|EMBL:AFC27530.1, ECO:0000313|Proteomes:UP000007523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3016 {ECO:0000313|EMBL:AFC27530.1};
RX   PubMed=22535950; DOI=10.1128/JB.00323-12;
RA   Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA   Shen D., Du B., Li J.;
RT   "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a
RT   Bacterium Functional as Microbial Fertilizer.";
RL   J. Bacteriol. 194:2777-2778(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP003235; AFC27530.1; -; Genomic_DNA.
DR   RefSeq; WP_014368382.1; NC_016935.1.
DR   ProteinModelPortal; H6NSY9; -.
DR   EnsemblBacteria; AFC27530; AFC27530; PM3016_563.
DR   KEGG; pmq:PM3016_563; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; PMUC1116391:GLI5-596-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007523; 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 {ECO:0000313|Proteomes:UP000007523};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007523}.
FT   DOMAIN      246    374       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   394 AA;  44240 MW;  2E3CCA6856248B0B CRC64;
     MDSFYRPTRV EISLDALRHN IGEFRRVLPE HVRMMAVVKA DAYGHGAVEV CREVLQCGVE
     YIAVAFLDEG LELRKAGITA PILVLGYTPP EGLETAWNHD ITLNLYTDEL LDAWERLGPR
     ERPLRIHIKV DTGMNRIGVT GEEQAVTLIE RALGIPGLQV EGLFTHYACA DEEDKSYTLQ
     QYARFQQVVE HFRSRGIEFP YVHAGNSAAA IDTPELTYNM VRLGISMYGL YPSDEVMKER
     VDLQPVLSIK TGVVMLKKVP AGEGISYGAV YRSQEEETIA TLPIGYADGF SRMLTGKAYA
     LIRGRRVPIV GRICMDQCMM NVTPLADISS EEEVVILGRQ GSETISAEEH AQWLGTVNYE
     VVCMISHRVP RMYIRGGQVV STINPLLRHL WERK
//
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