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Database: UniProt/TrEMBL
Entry: A0A0D6I3U2_ALCXX
LinkDB: A0A0D6I3U2_ALCXX
Original site: A0A0D6I3U2_ALCXX 
ID   A0A0D6I3U2_ALCXX        Unreviewed;       376 AA.
AC   A0A0D6I3U2; A0A0M7DVY2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   18-JUL-2018, entry version 24.
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=dadX_2 {ECO:0000313|EMBL:CKH79662.1};
GN   Synonyms=dadX_1 {ECO:0000313|EMBL:CUI38317.1};
GN   ORFNames=ERS369984_00498 {ECO:0000313|EMBL:CUI38317.1},
GN   ERS451415_03961 {ECO:0000313|EMBL:CKH79662.1};
OS   Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=85698 {ECO:0000313|EMBL:CKH79662.1, ECO:0000313|Proteomes:UP000059657};
RN   [1] {ECO:0000313|EMBL:CKH79662.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC10807 {ECO:0000313|EMBL:CKH79662.1};
RA   Informatics Pathogen;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CUI38317.1, ECO:0000313|Proteomes:UP000040179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608609 {ECO:0000313|EMBL:CUI38317.1,
RC   ECO:0000313|Proteomes:UP000040179};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-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; LN831029; CKH79662.1; -; Genomic_DNA.
DR   EMBL; CYTP01000001; CUI38317.1; -; Genomic_DNA.
DR   RefSeq; WP_006384296.1; NZ_PHGT01000001.1.
DR   ProteinModelPortal; A0A0D6I3U2; -.
DR   EnsemblBacteria; CKH79662; CKH79662; ERS451415_03961.
DR   EnsemblBacteria; CUI38317; CUI38317; ERS369984_00498.
DR   GeneID; 29505277; -.
DR   KEGG; axx:ERS451415_03961; -.
DR   PATRIC; fig|85698.19.peg.1030; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000040179; Unassembled WGS sequence.
DR   Proteomes; UP000059657; Chromosome 1.
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:UP000040179,
KW   ECO:0000313|Proteomes:UP000059657};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CKH79662.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      250    375       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    271    271       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     319    319       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  39460 MW;  F35BF0A2D9E9EF32 CRC64;
     MPRPISATVS VSALAHNLAA VRRHLDQTAA AASGVAPSIW AVIKANAYGH GIEQAVAGFS
     KAQGLAMLDL DEAVRCREAG WGGPILLLEG FFNPSDLDIV DRYHLSVTVH QREQLDMLAR
     ARLSRRVDIM LKLNSGMNRL GFSPAAYPAA HERALLLQQQ GVIGSLGKMT HFACADGPQG
     ITEQLAVFNS VTHKMAAGPI SVCNSAATLR FAEIAVGSEA QAHWVRPGIC LYGASPFADA
     EAAAFGLKPA MSLRSEIIAV QELKAGDSVG YGALFRADRP MRVGIVACGY ADGYPRHAAT
     GTPVVVAGIR TRLVGRVSMD MLIVDLDPIP AAGVGAPVSL WGEEGPSVDE VALAAGTIGY
     ELLCALAPRV PVTRDA
//
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