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Database: UniProt/TrEMBL
Entry: A0A0E0UBP1_SINMB
LinkDB: A0A0E0UBP1_SINMB
Original site: A0A0E0UBP1_SINMB 
ID   A0A0E0UBP1_SINMB        Unreviewed;       379 AA.
AC   A0A0E0UBP1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   07-JUN-2017, entry version 19.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=SinmeB_0751 {ECO:0000313|EMBL:AEG03685.1};
OS   Sinorhizobium meliloti (strain BL225C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=698936 {ECO:0000313|EMBL:AEG03685.1, ECO:0000313|Proteomes:UP000008709};
RN   [1] {ECO:0000313|Proteomes:UP000008709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL225C {ECO:0000313|Proteomes:UP000008709};
RX   PubMed=21569405; DOI=10.1186/1471-2164-12-235;
RG   US DOE Joint Genome Institute;
RA   Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S.,
RA   Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L.,
RA   Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D.,
RA   Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M.,
RA   Biondi E.G.;
RT   "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium
RT   Sinorhizobium meliloti.";
RL   BMC Genomics 12:235-235(2011).
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; CP002740; AEG03685.1; -; Genomic_DNA.
DR   RefSeq; WP_010969059.1; NC_017322.1.
DR   ProteinModelPortal; A0A0E0UBP1; -.
DR   SMR; A0A0E0UBP1; -.
DR   EnsemblBacteria; AEG03685; AEG03685; SinmeB_0751.
DR   KEGG; smq:SinmeB_0751; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   BioCyc; SMEL698936:GLK9-744-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008709; 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:UP000008709};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AEG03685.1};
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;  40234 MW;  DD8229ACDD963649 CRC64;
     MQSPEFLSAS SRLTVDLTAL ADNWRAMNER SGKARAAAVL KADAYGLGVV HAAPALYAAG
     ARDFFVASVE EGADLRPLVP DGRIYILAGM WPGNEELFFE NDLVPIINSE EQLAVFMAAL
     SERGDHPCVL HVDTGMNRLG LSPEEALALA HDPARPASFS PVLVMSHLAC ADDPGHPMNR
     YQLQRFREVT AAFEGVPASL ANSGGVFLGA DYHFDLTRPG IAVYGGEAVN GAVNPMKAVV
     TAEARIVQVR TVPSGGTASY GASVRFGRDS RIATVAIGYA DGYHRSVSGG GVTLRQAMPS
     GAFGFLHGMK VPHVGRVTMD LSLFDVTDLP EAAVRAGDYI EVFGRNVVID DVARAGGTIG
     YELLTSLGRR YHRTYVGGA
//
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