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Database: UniProt/TrEMBL
Entry: A0A0U3R2D5_9ACTN
LinkDB: A0A0U3R2D5_9ACTN
Original site: A0A0U3R2D5_9ACTN 
ID   A0A0U3R2D5_9ACTN        Unreviewed;       392 AA.
AC   A0A0U3R2D5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   20-JUN-2018, entry version 24.
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=ASR50_21645 {ECO:0000313|EMBL:ALV51754.1};
OS   Streptomyces sp. 4F.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1751294 {ECO:0000313|EMBL:ALV51754.1, ECO:0000313|Proteomes:UP000056717};
RN   [1] {ECO:0000313|EMBL:ALV51754.1, ECO:0000313|Proteomes:UP000056717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4F {ECO:0000313|EMBL:ALV51754.1,
RC   ECO:0000313|Proteomes:UP000056717};
RA   Jing X.;
RT   "The complete genome sequence of a mosephilic streptomyces 4F.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP013142; ALV51754.1; -; Genomic_DNA.
DR   RefSeq; WP_037641118.1; NZ_CP013142.1.
DR   EnsemblBacteria; ALV51754; ALV51754; ASR50_21645.
DR   KEGG; strf:ASR50_21645; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000056717; 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   Complete proteome {ECO:0000313|Proteomes:UP000056717};
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      259    386       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    280    280       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     328    328       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   392 AA;  40678 MW;  361C24F2E703F746 CRC64;
     MKETADPHGA QLRARAVIDL AAVRANVRTL RDRAPRAALM AVVKADGYGH GAAPCARAAV
     EAGATWLGTA TPQEALALRA PGSGVPDDVR VMCWLWTPGG PWREAVEADV DVSVSGFWAL
     DEVVAAARAA GRPARVQLKA DTGLGRGGCQ PADWAELVAG ALRAQAEGLL KVTGLWSHFA
     CADEPGHPSI AAQLLTFREM VAYAEAQGVE PEVRHIANSP ATLTLPESHF DLVRPGIAMY
     GVSPSPEIGT PVELGLRPAM TLSASLALVK NVPGGHGVSY GHHYVTAGAT TLGLVPLGYA
     DGIPRHASGG GPVLVEGKWR TVAGRVAMDQ FVVDLGGDEP GEGAEAVLFG PGDRGEPTAE
     DWAQASGTIA YEIVTRIGSR VPRVYVNGEQ SG
//
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