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Database: UniProt/TrEMBL
Entry: D4KXL8_9FIRM
LinkDB: D4KXL8_9FIRM
Original site: D4KXL8_9FIRM 
ID   D4KXL8_9FIRM            Unreviewed;       389 AA.
AC   D4KXL8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   28-FEB-2018, entry version 54.
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=RO1_14990 {ECO:0000313|EMBL:CBL12108.1};
OS   Roseburia intestinalis XB6B4.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Roseburia.
OX   NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL12108.1, ECO:0000313|Proteomes:UP000008953};
RN   [1] {ECO:0000313|EMBL:CBL12108.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12108.1,
RC   ECO:0000313|Proteomes:UP000008953};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Roseburia intestinalis XB6B4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL12108.1, ECO:0000313|Proteomes:UP000008953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12108.1,
RC   ECO:0000313|Proteomes:UP000008953};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929050; CBL12108.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4KXL8; -.
DR   STRING; 718255.RO1_14990; -.
DR   EnsemblBacteria; CBL12108; CBL12108; RO1_14990.
DR   KEGG; rix:RO1_14990; -.
DR   PATRIC; fig|718255.3.peg.2694; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008953; 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:UP000008953};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CBL12108.1};
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:UP000008953}.
FT   DOMAIN      247    375       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   389 AA;  43124 MW;  105B88A7385D065A CRC64;
     MNRYSRVHAE IDLDAILHNM DAMRGNIAKD TKIMAVIKAD GYGHGAVEIA ETIEKLDYLY
     GYAVATVEEG LILRNHGIQK PILILGYVFP DQYVDMIKAG IRPTVFTREM AEKLSVAAAS
     IGRDCKIHFA IDTGMSRIGY QVTEEATDEM AQLSKLPHII VEGIFTHFAK ADEKDKEPTY
     QQIKLFRKMI DMLEERGVSI PIHHCSNSAG IVDIPEANMD MVRAGITLYG MWPSEDVDKT
     AISLKPALSL VTHVAYVKEL PAGRAISYGG TYVTKEPRMI ATIPVGYADG YARGLSNKGA
     VLIHGRRAPI LGRVCMDQFM VDVTDIPDVK NEDEVILIGR DGDECITMEE VGGLSGRFNY
     EFACDLGKRI PRVYIHGGRI IGTRDHFSE
//
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