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Database: UniProt/TrEMBL
Entry: U4Q2R4_9RHIZ
LinkDB: U4Q2R4_9RHIZ
Original site: U4Q2R4_9RHIZ 
ID   U4Q2R4_9RHIZ            Unreviewed;       391 AA.
AC   U4Q2R4;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
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=BN877_I1068 {ECO:0000313|EMBL:CDI07979.1};
OS   Rhizobium sp. IRBG74.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=424182 {ECO:0000313|EMBL:CDI07979.1, ECO:0000313|Proteomes:UP000016944};
RN   [1] {ECO:0000313|EMBL:CDI07979.1, ECO:0000313|Proteomes:UP000016944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRBG74 {ECO:0000313|EMBL:CDI07979.1};
RX   PubMed=24265489; DOI=10.1128/genomeA.00934-13;
RA   Crook M.B., Mitra S., Ane J.M., Sadowsky M.J., Gyaneshwar P.;
RT   "Complete Genome Sequence of the Sesbania Symbiont and Rice Growth-
RT   Promoting Endophyte Rhizobium sp. Strain IRBG74.";
RL   Genome Announc. 1:e00934-e00913(2013).
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; HG518322; CDI07979.1; -; Genomic_DNA.
DR   RefSeq; WP_022555926.1; NC_022535.1.
DR   EnsemblBacteria; CDI07979; CDI07979; BN877_I1068.
DR   KEGG; rir:BN877_I1068; -.
DR   PATRIC; fig|424182.3.peg.1066; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; RSP424182:G13G6-1077-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000016944; 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:UP000016944};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CDI07979.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      250    387       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     52     52       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     330    330       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      52     52       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   391 AA;  42148 MW;  20A63011E24C93B4 CRC64;
     MTDDLEDTFA ETETDAFEHA PLRLTVDLGA LADNWRDMRR RSGKARTAAV VKADAYGLGI
     EDCGAALYHA GARDFFVATV AEGETLRSYA PEARIFVLSG IWQGQERQVF DNDLVPVLAS
     EEQLSFWMAT VAERGDHPCA LHVDTGFNRL GLPLDDALFL ADDVTRPASF DPVLVLSHLA
     CADTPSSPMN RAQLESFRMV STAFEGIESS LSASAGIFLG PDYHFDLTRP GIALYGGEAV
     NDVANPMRPV AKAEARIIQI RDAGEGQTVS YGGTFLLKRA SRLAIATVGY ADGYQRSLSG
     SGIPLREMGH GGAYGVVNGH KVPVAGRVTM DLTIFDVTDV PANAIRTGDY VELFGPNVPV
     DETARAAGTI GYEMLTGLGL RYERQYLMAD D
//
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