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Database: UniProt/TrEMBL
Entry: D4JPH2_9FIRM
LinkDB: D4JPH2_9FIRM
Original site: D4JPH2_9FIRM 
ID   D4JPH2_9FIRM            Unreviewed;       376 AA.
AC   D4JPH2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-SEP-2017, 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=ERE_32330 {ECO:0000313|EMBL:CBK94991.1};
OS   [Eubacterium] rectale M104/1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=657317 {ECO:0000313|EMBL:CBK94991.1, ECO:0000313|Proteomes:UP000008802};
RN   [1] {ECO:0000313|EMBL:CBK94991.1, ECO:0000313|Proteomes:UP000008802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M104/1 {ECO:0000313|EMBL:CBK94991.1,
RC   ECO:0000313|Proteomes:UP000008802};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Eubacterium rectale M104/1.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK94991.1, ECO:0000313|Proteomes:UP000008802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M104/1 {ECO:0000313|EMBL:CBK94991.1,
RC   ECO:0000313|Proteomes:UP000008802};
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; FP929043; CBK94991.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4JPH2; -.
DR   EnsemblBacteria; CBK94991; CBK94991; ERE_32330.
DR   KEGG; era:ERE_32330; -.
DR   PATRIC; fig|657317.3.peg.509; -.
DR   KO; K01775; -.
DR   BioCyc; EREC657317:G1362-2863-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008802; 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; 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:UP000008802};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CBK94991.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      246    374       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  41712 MW;  284144FD3D4454B5 CRC64;
     MAINRIRADI DLDAILYNME SMHNKLKPGT MMAAVVKADG YGHGAEAVSE VLEPLPYLWG
     YAVATSNEAM ELIAAGRKKP ILILGLSFPE QFEEIVDNDV RPAVCTYETA KELSRIAVAK
     NKTCKIHIKI DTGMCRIGFQ VTEESADIIA QIAKLPNIMI EGIFTHFARA DELSKEPAFE
     QFDLFKRMIA LVEAREVEIP IKHCSNSAGI VEIPECNMDM VRAGITLYGL WPSEEVDKSK
     ISLKPVMSLH SRVAYVKELE PGRHISYGGT FTVEHPMRIA TVPVGYGDGY SRGLSNKGWV
     LIKGKKAPIC GRVCMDQFMV DVTDIPDVKI GDAVTLLGKD GDETITMEQL GELSGRFNYE
     FACLITPRVP RIYHKN
//
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