GenomeNet

Database: UniProt/TrEMBL
Entry: Q2W5H6_MAGSA
LinkDB: Q2W5H6_MAGSA
Original site: Q2W5H6_MAGSA 
ID   Q2W5H6_MAGSA            Unreviewed;       409 AA.
AC   Q2W5H6;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   07-JUN-2017, entry version 93.
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=amb2095 {ECO:0000313|EMBL:BAE50899.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50899.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE50899.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y.,
RA   Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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}.
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}.
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; AP007255; BAE50899.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q2W5H6; -.
DR   STRING; 342108.amb2095; -.
DR   EnsemblBacteria; BAE50899; BAE50899; amb2095.
DR   KEGG; mag:amb2095; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; ISHFACA; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007058; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007058};
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:UP000007058}.
FT   DOMAIN      276    402       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     77     77       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    297    297       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     175    175       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     345    345       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      77     77       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   409 AA;  42845 MW;  6BBC9920F79A4B5C CRC64;
     MPGWASGNCA ATCAFAEQGL VFPSEERDGA LSPLPGRTMT DLARATALLT IDVAAIVANW
     KRLSALVAPA EASAVVKADC YGLGMDRIAP ALFAAGCRSF FVACVNEGIA LRRLLPGAMI
     HVLSGPMGGD EAEFAAHGLI PVLNSLSQMT GWASFAKKGS GAPAVAIHID TGMSRLGLSE
     PELERLAAKP EILAAMRPIL VMSHLACADD SDSPMNARQL TTLRRLASHL PALPQSIAAS
     SGIFLGRGFH LGMVRPGAAL YGLNPMPGRP NPMSQVIKLE GKIVQVRDVD SPQTVGYGAT
     HRVEGKRRLA IVAVGYADGW FRSLSNRGHG MIGGVKVPVV GRVSMDLTTF DVTDVPVESA
     HPGGLIQLIG PGYGPDHLAA EADTIGYEVL TALGRRHLRR WIGTEGAAS
//
DBGET integrated database retrieval system