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Database: UniProt/TrEMBL
Entry: A0A1S0R837_ENSAD
LinkDB: A0A1S0R837_ENSAD
Original site: A0A1S0R837_ENSAD 
ID   A0A1S0R837_ENSAD        Unreviewed;       379 AA.
AC   A0A1S0R837;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUL-2017, entry version 4.
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=FA04_04255 {ECO:0000313|EMBL:ANK71911.1};
OS   Ensifer adhaerens (Sinorhizobium morelense).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer.
OX   NCBI_TaxID=106592 {ECO:0000313|EMBL:ANK71911.1, ECO:0000313|Proteomes:UP000027454};
RN   [1] {ECO:0000313|EMBL:ANK71911.1, ECO:0000313|Proteomes:UP000027454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Casida A {ECO:0000313|EMBL:ANK71911.1,
RC   ECO:0000313|Proteomes:UP000027454};
RA   Baltrus D.A., Martin M.O., Williams L.E., O'donnell S.D.;
RT   "Complete Genome Sequence of the Predatory Bacteria Ensifer Adhaerens
RT   strain Casida A.";
RL   Submitted (MAY-2016) 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, 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; CP015880; ANK71911.1; -; Genomic_DNA.
DR   RefSeq; WP_034803986.1; NZ_CP015880.1.
DR   GeneID; 29517631; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000027454; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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:UP000027454};
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      239    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     41     41       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    260    260       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     319    319       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   379 AA;  40387 MW;  CBD0910D74439C30 CRC64;
     MLPPDFLSAS NRLTIDLGAL VDNWRAMNKR SGKARAAAVL KADAYGIGIA QAAPALYAAG
     ARDFFVANAE EGAALRPLAP DGRIYILAGM WPGNEALFFD NDLVPVINSD EQLAVFMAAL
     SERGDHPCVL HVDTGMNRLG LTVEQAVALA TDPARPASFS PVLIMSHLVS ADDPDHRLNG
     LQLRRFHEVS TAYEGVDASL ANSGGVFLGP DYHFDLTRPG IAVYGGEAVN DIPNPMKPVV
     TAEARIIQVR DVAAGGTASY GASARFDRDS RIATVAVGYA DGYHRSVSGG GVTLRQATPS
     GAFGFLHGQK VPHVGRVTMD LSLFDVTDLP ESAVRPGDYI ELFGRHIAID DVARAGGTIG
     YEMLTSLGRR YIRHYIDSV
//
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