GenomeNet

Database: UniProt/TrEMBL
Entry: F8E1W3_CORRG
LinkDB: F8E1W3_CORRG
Original site: F8E1W3_CORRG 
ID   F8E1W3_CORRG            Unreviewed;       559 AA.
AC   F8E1W3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-SEP-2017, entry version 50.
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:AEI10176.1};
GN   OrderedLocusNames=CRES_1823 {ECO:0000313|EMBL:AEI10176.1};
OS   Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI10176.1, ECO:0000313|Proteomes:UP000000492};
RN   [1] {ECO:0000313|EMBL:AEI10176.1, ECO:0000313|Proteomes:UP000000492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45100 / JCM 12819 / GTC 2026
RC   {ECO:0000313|Proteomes:UP000000492};
RX   PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA   Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA   Schneider J., Trost E., Tauch A.;
RT   "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT   human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT   samples of a leukemia patient.";
RL   BMC Genomics 13:141-141(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}.
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; CP002857; AEI10176.1; -; Genomic_DNA.
DR   RefSeq; WP_013889163.1; NC_015673.1.
DR   ProteinModelPortal; F8E1W3; -.
DR   STRING; 662755.CRES_1823; -.
DR   EnsemblBacteria; AEI10176; AEI10176; CRES_1823.
DR   KEGG; crd:CRES_1823; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   eggNOG; COG0802; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000492; 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   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000492};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AEI10176.1};
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:UP000000492}.
FT   DOMAIN      260    389       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    281    281       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     329    329       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   559 AA;  59434 MW;  A6BA8CD311A5C523 CRC64;
     MYQPLPVPAE HALAEVIIDL SAVRSNVSLF ADAAPSAEVM AVVKADAYNH GAFSVARACL
     ESGATQLGVA TIGEALSLRT AGITAPITAW MWIPGEDLSR AIQQDITIGV PSLAHAEALV
     ELVDTLEQSD SNSTPIAISL MADTGLSRSG ITPDQWATVV ELIAKYSASF DVRGVMSHLA
     SADDSARAAF TDVQNRRFQR AIEICREHGI DPRTNHIANT PAALTRPDLH HQMVRPGVGI
     YGIDPVVGGS GGNAGQLRPA ITFRAKVITT KTIRAGESVS YGGTWTATRD TRTAVVAAGY
     ADGVPRAASG KFHVGIGGKL YPQIGRVCMD QIVVNLGDSE EPTDVKPGDW ATIFGEGGIS
     ASELAAAAET IDYEILTMPR GPRVWRRWVG EEKEQLDLSH SNGHATASTS EDMVEAGRRI
     GEQLEAGTVV VLTGPLGAGK TTLTQGLAAG LEVKGRVQSP TFTIVRTHKP SGSGRPGMLH
     MDAYRLLGAD VSEGVEPGKH VDRDVVLDAL ESLDIDSDLD QVVVIAEWGR GVVETLSDKV
     LDIEIDRAAD ERILRWEWK
//
DBGET integrated database retrieval system