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Database: UniProt/TrEMBL
Entry: A0A1U9RTY2_CORPS
LinkDB: A0A1U9RTY2_CORPS
Original site: A0A1U9RTY2_CORPS 
ID   A0A1U9RTY2_CORPS        Unreviewed;       370 AA.
AC   A0A1U9RTY2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
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:AQU92111.1};
GN   ORFNames=CpMIC6_0441 {ECO:0000313|EMBL:AQU92111.1};
OS   Corynebacterium pseudotuberculosis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1719 {ECO:0000313|EMBL:AQU92111.1, ECO:0000313|Proteomes:UP000189657};
RN   [1] {ECO:0000313|EMBL:AQU92111.1, ECO:0000313|Proteomes:UP000189657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIC6 {ECO:0000313|EMBL:AQU92111.1,
RC   ECO:0000313|Proteomes:UP000189657};
RA   Sousa T., Mariano D., Ibraim I.C., Sousa F., Bagano P., Ramos R.,
RA   Almeida S., Silva A., Azevedo V.A.C.;
RT   "Complete Genome Sequencing of Corynebacterium pseudotuberculosis
RT   strain MIC6.";
RL   Submitted (FEB-2017) 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}.
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}.
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DR   EMBL; CP019769; AQU92111.1; -; Genomic_DNA.
DR   RefSeq; WP_013241268.1; NZ_CP020356.1.
DR   KEGG; cpse:CPTA_00951; -.
DR   KEGG; cpsf:CPTC_00242; -.
DR   KEGG; cpsu:CPTB_00582; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000189657; 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; 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:UP000189657};
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      241    367       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     36     36       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   370 AA;  39926 MW;  0C2920E487111667 CRC64;
     MNLLEARIDL AAIAHNTRLI KDKAAAQGAQ LMCVVKADGY NHGAVEVATV MEENGADQFG
     VATIGEALAL REGGIESSIL SWIWSPEQDL GAAITAEIDL AAISLEHVKA LVRASESYGK
     KPVRVTVKVD TGLHRSGVDK QDWRESFCML RDAENIQVTG VFSHFSSADE SDSTETEQQE
     RAFLNAIELG RSLGLELPVN HIANSPATLN RPDLYFDMVR PGLALYGHEP IPGESHGLRE
     AMSWVGRVTV VKPIARGEGT SYGLTWRAEQ DGYLCVVPVG YADGLPRSAQ GHLEITIGGR
     RYPQVGRVCM DQIVVALGEN PYGVAQGDEA VILGPTGMTA TELATAMGTI NYELVCRPCG
     RTVRVFEHSD
//
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