GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0U3BN09_STRGL
LinkDB: A0A0U3BN09_STRGL
Original site: A0A0U3BN09_STRGL 
ID   A0A0U3BN09_STRGL        Unreviewed;       384 AA.
AC   A0A0U3BN09;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-FEB-2018, entry version 15.
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=WQO_21645 {ECO:0000313|EMBL:ALU98231.1};
OS   Streptomyces globisporus C-1027.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU98231.1};
RN   [1] {ECO:0000313|EMBL:ALU98231.1, ECO:0000313|Proteomes:UP000064183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-1027 {ECO:0000313|EMBL:ALU98231.1,
RC   ECO:0000313|Proteomes:UP000064183};
RX   PubMed=22815456; DOI=10.1128/JB.00797-12;
RA   Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT   "Draft genome sequence of Streptomyces globisporus C-1027, which
RT   produces an antitumor antibiotic consisting of a nine-membered
RT   enediyne with a chromoprotein.";
RL   J. Bacteriol. 194:4144-4144(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, 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 https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013738; ALU98231.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALU98231; ALU98231; WQO_21645.
DR   KEGG; sgb:WQO_21645; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000064183; 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; -; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000064183};
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}.
FT   DOMAIN      244    371       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED        2     22       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     313    313       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   384 AA;  39939 MW;  17A454AEB817EFD1 CRC64;
     MRARAEIDLA ALRANVRVLR ERAAGAQLMA VVKSDGYGHG AVPCARAARA AGAAWLGTAT
     PHEALALRAA GLDGRIMCWL WTPGGPWREA IEADIDVSAG GMWALREIVA AAQAAGRPAR
     VQLKADTGLG RGGCQPADWP ELVGAARDAE RAGHLRITGL WSHFACADEP GHPSIAAQLA
     VYRDLVAYAE KEGVEPEVRH LANSPATLTI PEAHFDLVRT GIAMYGISPA PELGTSAELG
     LRPVMTLAAA VALVKDAPAG HGVSYGHHYT TPADTTLGLI PVGYADGVPR HASGSGPVLV
     GGKVRTVAGR VAMDQFVVDL EGDRPEAGAE AVLFGPGDRG EPTAQDWAEA AGTIAYEIVT
     RIGARVPRVY VNETADEVTG GVPR
//
DBGET integrated database retrieval system