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Database: UniProt/TrEMBL
Entry: K0ETG7_9NOCA
LinkDB: K0ETG7_9NOCA
Original site: K0ETG7_9NOCA 
ID   K0ETG7_9NOCA            Unreviewed;       369 AA.
AC   K0ETG7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-SEP-2017, entry version 35.
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:AFT98960.1};
GN   ORFNames=O3I_004990 {ECO:0000313|EMBL:AFT98960.1};
OS   Nocardia brasiliensis ATCC 700358.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFT98960.1, ECO:0000313|Proteomes:UP000006304};
RN   [1] {ECO:0000313|EMBL:AFT98960.1, ECO:0000313|Proteomes:UP000006304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUJEG-1 {ECO:0000313|EMBL:AFT98960.1};
RX   PubMed=22535940; DOI=10.1128/JB.00210-12;
RA   Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R.,
RA   Perez-Maya A.A., Ocampo-Candiani J.;
RT   "Complete genome sequence of Nocardia brasiliensis HUJEG-1.";
RL   J. Bacteriol. 194:2761-2762(2012).
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; CP003876; AFT98960.1; -; Genomic_DNA.
DR   ProteinModelPortal; K0ETG7; -.
DR   EnsemblBacteria; AFT98960; AFT98960; O3I_004990.
DR   KEGG; nbr:O3I_004990; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006304; 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:UP000006304};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AFT98960.1};
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:UP000006304}.
FT   DOMAIN      237    365       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     31     31       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      31     31       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   369 AA;  39203 MW;  AADE0AB67DF4ABB5 CRC64;
     METVVDLDAI AHNVRILREL AGDAAVMAVV KADGYNHGAV EVGKAALAAG AAELGVTTIA
     EAVRLREAGI TAPILSWLNN SAADYAAAIG ADIEIGVSSL DHLRAVAAAT EQTGRTATVS
     LKVDTGLNRN GLSPVEYPQA LAELRTLVDA QAMRFRALFS HLANADEPAH PVNDMQRDRF
     LEAIAVAKEH GLEPELVHLA NSPATLTRPD LAFDMVRPGI AMYGHSPVAE DFGLRPAMTF
     QARVALVKQV AAGEGVSYGH TWYAPRDTTV ALIPVGYADG VFRPLSGRFE VWLGGARRPN
     VGRVCMDQFV VDLGDNAANV REGDMAVLFG GGPGEPRAQE WADLLGTIHY EVVCSPRGRS
     VRRYVGGGR
//
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