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Database: UniProt/TrEMBL
Entry: A0A068T4G4_RHIGA
LinkDB: A0A068T4G4_RHIGA
Original site: A0A068T4G4_RHIGA 
ID   A0A068T4G4_RHIGA        Unreviewed;       387 AA.
AC   A0A068T4G4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-SEP-2017, entry version 23.
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=RG1141_CH10130 {ECO:0000313|EMBL:CDN53372.1};
OS   Neorhizobium galegae bv. officinalis bv. officinalis str. HAMBI 1141.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Neorhizobium.
OX   NCBI_TaxID=1028801 {ECO:0000313|EMBL:CDN53372.1, ECO:0000313|Proteomes:UP000028186};
RN   [1] {ECO:0000313|Proteomes:UP000028186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 1141 {ECO:0000313|Proteomes:UP000028186};
RA   Oesterman J., Marsh J., Laine P.K., Alatalo E., Sullivan J.,
RA   Young J.P.W., Thomas-Oates J., Paulin L., Lindstroem K.;
RT   "Genome sequencing of two Neorhizobium galegae strains reveals a noeT
RT   gene responsible for the unusual acetylation of the nodulation
RT   factors.";
RL   BMC Genomics 15:500-500(2014).
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; HG938355; CDN53372.1; -; Genomic_DNA.
DR   RefSeq; WP_038541646.1; NZ_HG938355.1.
DR   EnsemblBacteria; CDN53372; CDN53372; RG1141_CH10130.
DR   KEGG; ngl:RG1141_CH10130; -.
DR   PATRIC; fig|1028801.3.peg.1037; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000028186; Chromosome I.
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:UP000028186};
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}.
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   387 AA;  41740 MW;  475E2ABDBBDAF393 CRC64;
     MTDFDSELSY PDDFDIAPVR LTVDLGALGD NWREMARRSG TARTAAVVKA DAYGLGLEDC
     GITLYEAGAR DFFVAVVQEG VTLRTYAPDA RIYVLSGIWP GQERMFFEHD LVPVLASEEQ
     LAFWMSVTAE YGDHPCALQV DTGFNRLGLP LEDAIAFSDD VSRPASFSPV LVLSHLHSGD
     TPSSPLNQKQ LSAFQKVAEA FEGIETSLSA SAGIFLGPDY HFDLTRPGIA LYGGEAVVGV
     PNPMKPVAKA EARIIQIRDG KKGETVSYGG TYQLSRDSRL AIVSAGYADG YKRALSGSGV
     PLRQTIGQGG FGFIAGREVP VIGRITMDLT IFDVTDIPAS DIQAGDYVEL FGPNVALDDV
     ARAAGTIGYE LLTSLGLRYE RRYIEAE
//
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