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Database: UniProt/TrEMBL
Entry: A0A0K2GYK0_9CORY
LinkDB: A0A0K2GYK0_9CORY
Original site: A0A0K2GYK0_9CORY 
ID   A0A0K2GYK0_9CORY        Unreviewed;       550 AA.
AC   A0A0K2GYK0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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=CLAC_02295 {ECO:0000313|EMBL:ALA66748.1};
OS   Corynebacterium lactis RW2-5.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1408189 {ECO:0000313|EMBL:ALA66748.1};
RN   [1] {ECO:0000313|EMBL:ALA66748.1, ECO:0000313|Proteomes:UP000058446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW2-5 {ECO:0000313|EMBL:ALA66748.1,
RC   ECO:0000313|Proteomes:UP000058446};
RA   Ruckert C., Albersmeier A., Lipski A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium lactis DSM 45799(T),
RT   isolated from raw cow milk.";
RL   Submitted (OCT-2013) 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; CP006841; ALA66748.1; -; Genomic_DNA.
DR   RefSeq; WP_053411515.1; NZ_CP006841.1.
DR   EnsemblBacteria; ALA66748; ALA66748; CLAC_02295.
DR   KEGG; clw:CLAC_02295; -.
DR   PATRIC; fig|1408189.4.peg.455; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000058446; 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   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000058446};
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      263    391       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     45     45       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    284    284       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     332    332       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      45     45       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   550 AA;  58267 MW;  5DD789093A648C6F CRC64;
     MTSSQSPQPT VQPLLTQTVN LDAVAHNVAT IKQISGVDEF MAVVKADGYS QGATQVARAA
     IGGGATQLGV ATLEEALSLC AALSDPLADA PAVPILAWIW DAAAVDLVRQ AVEQEIELGI
     PSVAHAHAVA QAGAVLGRRP RVTVMVDTGL GRSGISMANG DFDVAVGEVA QLHAEEKLLV
     TGLFTHFACA DEPQHPSVDR QAENFRAAIA ALREAGVEGL VNHAANSPAA LERPDLAFDM
     VRPGLAIYGG EPVAGARHGL RPVMRWEAAV VLVKKLPKGE SVSYGLTWTA DRDTTVAVVP
     CGYADGMMRS ASGRFEVSID GKRYPQVGRV CMDQFVVDLG PDSDVRTGDI AVIVGDPELG
     EPGLDELANA SGTINYEILT APKGRTQRHW VHSRVVPTAE DMRYLGEEIG RTLRGGDLVI
     MDGPLGAGKT TMTQGIARGM NVRGRVTSPT FTIAREHRPL DDGAPLIHVD AYRLFGEEGP
     DSDGAAEPSA ISAFDALDSL DLDTELEDSV VVAEWGTGLA EQLAENYLRI TIDRSRADDT
     RVVTWAWSRG
//
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