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Database: UniProt/TrEMBL
Entry: U6B3U5_9RHIZ
LinkDB: U6B3U5_9RHIZ
Original site: U6B3U5_9RHIZ 
ID   U6B3U5_9RHIZ            Unreviewed;       350 AA.
AC   U6B3U5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 28.
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:AHA27714.1};
GN   ORFNames=lam_344 {ECO:0000313|EMBL:AHA27714.1};
OS   Candidatus Liberibacter americanus str. Sao Paulo.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1261131 {ECO:0000313|EMBL:AHA27714.1, ECO:0000313|Proteomes:UP000017862};
RN   [1] {ECO:0000313|EMBL:AHA27714.1, ECO:0000313|Proteomes:UP000017862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sao Paulo {ECO:0000313|EMBL:AHA27714.1};
RX   PubMed=24200077; DOI=10.1094/MPMI-09-13-0292-R;
RA   Wulff N.A., Zhang S., Setubal J.C., Almeida N.F., Martins E.C.,
RA   Harakava R., Kumar D., Rangel L.T., Foissac X., Bove J., Gabriel D.W.;
RT   "The complete genome sequence of Candidatus Liberibacter americanus,
RT   associated with citrus Huanglongbing.";
RL   Mol. Plant Microbe Interact. 27:163-176(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; CP006604; AHA27714.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHA27714; AHA27714; lam_344.
DR   KEGG; lar:lam_344; -.
DR   PATRIC; fig|1261131.3.peg.332; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000017862; 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:UP000017862};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017862}.
FT   DOMAIN      215    350       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     15     15       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    236    236       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     112    112       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     295    295       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      15     15       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   350 AA;  38438 MW;  9D9BBD21A982A450 CRC64;
     MNKLSGNART AAVVKDNAYG LGLEQISKSL YKAGAKDFFV KNIEEGIKLR DYVKKANIFV
     LSEDNIGQER SLIEANLIPV LYSSNQLKLY SQLLSNHQSH CYALQIDTGF NRLGLSIDEA
     LSFAENFDNK NQINNKLSLI ISHLACAENQ NSPMNASQLN KFMSIATKYQ GIEASLSASA
     GIFLGKEYHF QLTRPGIALY GGTYAINKLH PMRTVVTAEA RIILIRTANA GEIVSYGGEK
     KLKRNSLIAV AAIGYCDGYP LSLSGIDHKD NISINNVGQG FIKGYKVPIL GKITMDMTMF
     DITDCPGIEV GDYIQVFGPN IKLDDVANAS GTTNYELLVQ IGNKYARHYI
//
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