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Database: UniProt/TrEMBL
Entry: A0A0U3GKD6_9MICC
LinkDB: A0A0U3GKD6_9MICC
Original site: A0A0U3GKD6_9MICC 
ID   A0A0U3GKD6_9MICC        Unreviewed;       405 AA.
AC   A0A0U3GKD6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-FEB-2018, entry version 14.
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=AS188_13795 {ECO:0000313|EMBL:ALU40638.1};
OS   Kocuria flava.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU40638.1, ECO:0000313|Proteomes:UP000057181};
RN   [1] {ECO:0000313|EMBL:ALU40638.1, ECO:0000313|Proteomes:UP000057181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO-9041 {ECO:0000313|EMBL:ALU40638.1,
RC   ECO:0000313|Proteomes:UP000057181};
RA   Zhou M., Dai J.;
RT   "Complete Genome Sequence of Kocuria flava strain HO-9041.";
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; CP013254; ALU40638.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALU40638; ALU40638; AS188_13795.
DR   KEGG; kfv:AS188_13795; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000057181; 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:UP000057181};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057181}.
FT   DOMAIN      263    393       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     48     48       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     145    145       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     331    331       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   405 AA;  41174 MW;  3528B0E899A8571F CRC64;
     MSSPAPSVPL PPAGAPERSA VVDLAAVRAN VRRAREVAAP ARLMAVVKAD AYGHGAVPVA
     RAALAAGADA LGVAHVAEAL QLRAAGVDAP LLAWLHTVGT DFRAGLAAGV ELGVSGWELA
     PIAEAARALG TTARIHLKID TGLGRNGATE AAWPGLVRAA AAAEAEGLVE VVGIFTHLAV
     ADEPERPETA QQLARFRAAV DAARAAGLRP ATRHAANSPG LFTARDQERP EDMLLDMVRV
     GVCLYGLSPF ADRTPEELGL VPAMTLRTTV SAVKEVPAGQ GVSYGLAHVT DRPTTLALVP
     LGYADGVPRA ATGGPVRIQG RTCPVVGRVA MDQVVVDLGA PGLAAPEHGL LGAEAVLFGA
     GENPSATAWA EAAGTINYEI VTRVSPRVPR VHVDGAPAGA GKEAP
//
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