GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1L3LKC9_9RHIZ
LinkDB: A0A1L3LKC9_9RHIZ
Original site: A0A1L3LKC9_9RHIZ 
ID   A0A1L3LKC9_9RHIZ        Unreviewed;       379 AA.
AC   A0A1L3LKC9;
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   Name=alr {ECO:0000313|EMBL:APG90506.1};
GN   ORFNames=SAMCFNEI73_Ch1192 {ECO:0000313|EMBL:APG90506.1};
OS   Sinorhizobium americanum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=194963 {ECO:0000313|EMBL:APG90506.1, ECO:0000313|Proteomes:UP000182306};
RN   [1] {ECO:0000313|EMBL:APG90506.1, ECO:0000313|Proteomes:UP000182306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFNEI 73 {ECO:0000313|EMBL:APG90506.1,
RC   ECO:0000313|Proteomes:UP000182306};
RA   Peralta H., Aguilar-Vera A., Diaz R., Mora Y., Martinez-Batallar G.,
RA   Salazar E., Vargas-Lagunas C., Encarnacion S., Girard L., Mora J.;
RT   "Genomic differences between typical nodule nitrogen-fixing rhizobial
RT   strains and those coming from bean seeds.";
RL   Submitted (OCT-2015) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013107; APG90506.1; -; Genomic_DNA.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000182306; 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:UP000182306};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:APG90506.1};
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;  40387 MW;  DBC91A04ED500651 CRC64;
     MHSPEFLAAS NRLTIDLTAL ADNWRAMNER SGKARAAAVL KADAYGIGVA HAAPTLYAAG
     ARDFFVADAE EGAELRPLLP DARIYILAGM WPGNEELFFA NDLVPIINSE EQLAGFMAAL
     SERGDHPCVL HVDTGMNRLG LSVEEAVALA HDPARPASFS PVLVMSHLAC GDDPKHPMNL
     YQLQRFREVA AAFEGVPASL ANSGGVFLGG DYHFDLTRPG IAVYGGEAVN DAVNPMKPVV
     TAEARILQLR TVPSGGTASY GASARFTRDS RIATVAIGYA DGYHRSVSGG GVTLRQAMPS
     GAFGFLHGRK VPHVGRVTMD LSLFDVTDLP ERAVRAGDYI ELFGRNVAID DVARAGGTIG
     YELLTSLGHR YCRTYVCGA
//
DBGET integrated database retrieval system