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Database: UniProt/TrEMBL
Entry: I3X0N9_RHIFR
LinkDB: I3X0N9_RHIFR
Original site: I3X0N9_RHIFR 
ID   I3X0N9_RHIFR            Unreviewed;       403 AA.
AC   I3X0N9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-SEP-2017, entry version 40.
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:AFL49445.1};
GN   ORFNames=USDA257_c08530 {ECO:0000313|EMBL:AFL49445.1};
OS   Sinorhizobium fredii USDA 257.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1185652 {ECO:0000313|EMBL:AFL49445.1, ECO:0000313|Proteomes:UP000006180};
RN   [1] {ECO:0000313|EMBL:AFL49445.1, ECO:0000313|Proteomes:UP000006180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA257 {ECO:0000313|Proteomes:UP000006180};
RX   PubMed=22843606; DOI=10.1128/JB.00966-12;
RA   Schuldes J., Rodriguez Orbegoso M., Schmeisser C., Krishnan H.B.,
RA   Daniel R., Streit W.R.;
RT   "Complete Genome Sequence of the Broad-Host-Range Strain Sinorhizobium
RT   fredii USDA257.";
RL   J. Bacteriol. 194:4483-4483(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; CP003563; AFL49445.1; -; Genomic_DNA.
DR   ProteinModelPortal; I3X0N9; -.
DR   EnsemblBacteria; AFL49445; AFL49445; USDA257_c08530.
DR   KEGG; sfd:USDA257_c08530; -.
DR   PATRIC; fig|1185652.3.peg.886; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006180; 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:UP000006180};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AFL49445.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      263    400       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     65     65       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    284    284       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     343    343       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      65     65       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   403 AA;  43142 MW;  46E052A347E2183B CRC64;
     MPKPFAASGA WMYCSRYRPC KSSPMHSPEF LAASNRLTID LTALADNWRA MNERSGKARA
     AAVLKANAYG IGVAHAAPAL CAAGARDFFV ADAEEGAELR PLLPDARIYI LAGMWPGNEE
     LFFANDLVPI INSEEQLAVF MATLSERGEH PCVLHVDTGM NRLGLSVEEA IALAHDPARP
     ASFSPVLVMS HLACGDDPKH PMNLYQLQRF REVTAAFEGV PASLANSGGV FLGEDYHFDL
     TRPGIAVYGG EAVNDAINPM KPVVTAEARI LQLRTVPSGG TASYGASARF TRDSRIATVA
     IGYADGYHRS VSGGGVTLRQ AMPSGAFGFL HGRKVPHVGR VTMDLSLFDV TDLPERAVRA
     GDYIELFGRN VAIDDVARAG GTIGYELLTS LGHRYCRTYA GGA
//
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