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Database: UniProt/TrEMBL
Entry: W6R719_9RHIZ
LinkDB: W6R719_9RHIZ
Original site: W6R719_9RHIZ 
ID   W6R719_9RHIZ            Unreviewed;       388 AA.
AC   W6R719;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-SEP-2017, entry version 29.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:CDM57057.1};
GN   ORFNames=LPU83_1384 {ECO:0000313|EMBL:CDM57057.1};
OS   Rhizobium favelukesii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=348824 {ECO:0000313|EMBL:CDM57057.1, ECO:0000313|Proteomes:UP000019443};
RN   [1] {ECO:0000313|EMBL:CDM57057.1, ECO:0000313|Proteomes:UP000019443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPU83 {ECO:0000313|EMBL:CDM57057.1,
RC   ECO:0000313|Proteomes:UP000019443};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Draft genome sequence of the broad-host-range Rhizobium sp. LPU83
RT   strain, a member of the low-genetic diversity Oregon-like Rhizobium
RT   sp. group.";
RL   Submitted (NOV-2013) 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:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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}.
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DR   EMBL; HG916852; CDM57057.1; -; Genomic_DNA.
DR   RefSeq; WP_024316457.1; NZ_HG916852.1.
DR   EnsemblBacteria; CDM57057; CDM57057; LPU83_1384.
DR   KEGG; rhl:LPU83_1384; -.
DR   PATRIC; fig|348824.6.peg.1490; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000019443; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019443};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CDM57057.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      247    384       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     49     49       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     327    327       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      49     49       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   388 AA;  42194 MW;  70CC2776B0B8AD75 CRC64;
     MTDFIDSFED EDPFDSAGLR LTVDLTALTE NWKDMARRSA KARAAAVVKA DAYGTGIEDS
     GEALYMAGAR DFFVATVDEG VTLRPYAPDA RIFVLSGIWP GTERRLFEND LVPVISSEEQ
     LAFWMAVLAE YGDYPCALNV DTGFNRLGLS MDEAIALADD VSRPASFAPV LVMSHLACSD
     DHSSEMNRQQ LESFRQVSAA YEGIDSSLAA SAGIFLGSDY HFDLTRPGIA LYGGESVNDM
     VNPMRPVVSA EARIIQVRTV KEGESVGYGR ATRLTRDSRL AIVSAGYADG YLRSQSSAGV
     PLRQTVPRGG QGFVAGRKVP VAGRISMDLT IFDVTDLPEN AVRAGDYVEL FGKNVLVDDV
     ARSAGTIGYE ILTSIGLRHE RRYLHEED
//
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