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Database: UniProt/TrEMBL
Entry: A0A143CDF2_9ACTN
LinkDB: A0A143CDF2_9ACTN
Original site: A0A143CDF2_9ACTN 
ID   A0A143CDF2_9ACTN        Unreviewed;       388 AA.
AC   A0A143CDF2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   20-DEC-2017, entry version 11.
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=A4E84_24490 {ECO:0000313|EMBL:AMW15477.1};
OS   Streptomyces sp. S10(2016).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1783515 {ECO:0000313|EMBL:AMW15477.1, ECO:0000313|Proteomes:UP000076096};
RN   [1] {ECO:0000313|EMBL:AMW15477.1, ECO:0000313|Proteomes:UP000076096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S10 {ECO:0000313|EMBL:AMW15477.1,
RC   ECO:0000313|Proteomes:UP000076096};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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}.
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DR   EMBL; CP015098; AMW15477.1; -; Genomic_DNA.
DR   RefSeq; WP_062931591.1; NZ_CP015098.1.
DR   EnsemblBacteria; AMW15477; AMW15477; A4E84_24490.
DR   KEGG; stsi:A4E84_24490; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000076096; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076096};
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      255    382       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   COILED       12     32       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     43     43       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    276    276       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     324    324       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      43     43       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   388 AA;  40321 MW;  F2C32FB569138587 CRC64;
     MSERTAPTAP LRARAEIDLA ALRANVRALR AHAPGAAVMA VVKSEAYGHG AVPCARAAVA
     AGASWLGTAT PEEALALRAA GLPGRIMCWL WTPGGPWREA IEADLDVSVS GMWALAEAVG
     AARGADRPAR VQLKADTGLG RGGCQPGADW AGLVREALRA EAEGLLRVTG LWSHFACADE
     PGHPSIADQL GVFREMVAYA EGQGVRPEVR HIANSPATLT LPESHFDLVR TGIATYGISP
     SPELGTPADF GLRPVMTLSG SLALVKHVPG GHGVSYGHRY VTPGATTLGL VPLGYADGIP
     RHASSAGPVL VEGKWRTIAG RVAMDQFVVD LGGDEPAAGA EAVLFGPGDR GEPTAEDWAQ
     AAGTIAYEIV TRIGTRVPRV YVNEERDG
//
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