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Database: UniProt/TrEMBL
Entry: W8T4F7_PEPAC
LinkDB: W8T4F7_PEPAC
Original site: W8T4F7_PEPAC 
ID   W8T4F7_PEPAC            Unreviewed;       385 AA.
AC   W8T4F7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   28-FEB-2018, entry version 25.
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:AHM55700.1};
GN   ORFNames=EAL2_c03970 {ECO:0000313|EMBL:AHM55700.1};
OS   Peptoclostridium acidaminophilum DSM 3953.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Peptoclostridium.
OX   NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM55700.1, ECO:0000313|Proteomes:UP000019591};
RN   [1] {ECO:0000313|EMBL:AHM55700.1, ECO:0000313|Proteomes:UP000019591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM55700.1,
RC   ECO:0000313|Proteomes:UP000019591};
RX   PubMed=24926057;
RA   Poehlein A., Andreesen J.R., Daniel R.;
RT   "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT   acidaminophilum al-2 (DSM 3953).";
RL   Genome Announc. 2:e00573-14(2014).
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; CP007452; AHM55700.1; -; Genomic_DNA.
DR   RefSeq; WP_025434738.1; NZ_CP007452.1.
DR   EnsemblBacteria; AHM55700; AHM55700; EAL2_c03970.
DR   KEGG; eac:EAL2_c03970; -.
DR   PATRIC; fig|1286171.3.peg.338; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000019591; 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:UP000019591};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AHM55700.1};
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:UP000019591}.
FT   DOMAIN      246    371       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    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      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   385 AA;  42751 MW;  6F4A41C5532A2AEA CRC64;
     MKYKNRPWAE INVENLRENF RNIKSLTKEG TKVCAVVKAN AYGHGSVQVA KILIEEGADY
     LAVASEGEAI ELRQAGIKTP ILCLGFVPEV VYEEAIANEL DITIYSLDAA EKLSKEAVRL
     GKNARVHIKL DTGMSRLGFQ VEDASVDAIE KIVGMPGIEL VGVFTHFAKA DEKDKTFTEH
     QYDGYMKIVS EVEKRGVKIQ IKHVCNSAGT MDMPQYHMDM VRPGIILYGL YPSDEVMKER
     LELKPVMTFK ASVSHVKDLE AGRGIGYGLR YVTEKTTRVA TMPIGYADGF TRMLSGKVSV
     KVNGTVVPVI GNICMDQSML NVDAVETKVG DEVVIFGEDI DARVERIAQA LGTINYEIVC
     MVARRIPRVY MEKNTVLQVV DYLVE
//
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