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Database: UniProt/TrEMBL
Entry: A0A0G3HH03_9CORY
LinkDB: A0A0G3HH03_9CORY
Original site: A0A0G3HH03_9CORY 
ID   A0A0G3HH03_9CORY        Unreviewed;       371 AA.
AC   A0A0G3HH03;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, 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   Name=alr {ECO:0000313|EMBL:AKK10432.1};
GN   ORFNames=CUTER_02085 {ECO:0000313|EMBL:AKK10432.1};
OS   Corynebacterium uterequi.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK10432.1, ECO:0000313|Proteomes:UP000035548};
RN   [1] {ECO:0000313|Proteomes:UP000035548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium uterequi DSM 45634,
RT   isolated from the uterus of a maiden mare.";
RL   Submitted (MAY-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; CP011546; AKK10432.1; -; Genomic_DNA.
DR   RefSeq; WP_047259021.1; NZ_CP011546.1.
DR   EnsemblBacteria; AKK10432; AKK10432; CUTER_02085.
DR   KEGG; cut:CUTER_02085; -.
DR   PATRIC; fig|1072256.5.peg.411; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000035548; 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   Complete proteome {ECO:0000313|Proteomes:UP000035548};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AKK10432.1};
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:UP000035548}.
FT   DOMAIN      240    366       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    261    261       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     309    309       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   371 AA;  38828 MW;  7865CB83C842290E CRC64;
     MSRPQLRVRV NLAAIAHNTR TLAGRLGPTT RLMAVVKADG YGHGAVAVAK TMADYGAEAF
     GVATIAEALQ LRDAGITEPI LAWLWQTGDD LSDAAAAGIE LAVPSPEHLQ ALVTSGLGLD
     VCLKVETGMH RSGLDESQWA DAFALAAANP QLRVTGLMSH LACADEPEHP ATDAQAAAFR
     RAIDAARVAG LAVPRNHLAN SAATLTRPDL HFEQVRVGLA LYGLNPMAAG VTPAAELQPA
     MTWEADVVAV KTVHPGDHVS YGWTYEAPAV AHTAVVPVGY ADGLPRRLQG NVEVTIGQRR
     YPQVGRVCMD QIVVNVGDNS DGVRPGDTAV LFGPGGAGVD EVADALGTIN YEALCLPKGR
     SQRVYEGGDH A
//
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