GenomeNet

Database: UniProt/SWISS-PROT
Entry: ALR2_CALS4
LinkDB: ALR2_CALS4
Original site: ALR2_CALS4 
ID   ALR2_CALS4              Reviewed;         388 AA.
AC   Q8R860;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   05-DEC-2018, entry version 106.
DE   RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr2; OrderedLocusNames=TTE2168;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 /
OS   JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AE008691; AAM25327.1; -; Genomic_DNA.
DR   RefSeq; WP_011026254.1; NC_003869.1.
DR   ProteinModelPortal; Q8R860; -.
DR   SMR; Q8R860; -.
DR   STRING; 273068.TTE2168; -.
DR   EnsemblBacteria; AAM25327; AAM25327; TTE2168.
DR   KEGG; tte:TTE2168; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; TTEN273068:G1FZJ-2271-MONOMER; -.
DR   BRENDA; 5.1.1.1; 6784.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000555; 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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    388       Alanine racemase 2.
FT                                /FTId=PRO_0000114589.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   388 AA;  43755 MW;  7C55CCEFF847BEEF CRC64;
     MFDEIRPTRV EVNLDSIVHN FREIKRVVGD RVKVMGVVKA NAYGHGAYHV AKALVENGVD
     YLAVATVEEA LELRSYGITA PVLILGYTPL SQAGEAVEKD VTFTAFDLKY VKELGEIASR
     KGKKAKIHVK IDTGMGRIGY TDFDLAEREI EEMSKLEGIE LEGIFSHFAT SDEKDKDYAR
     EQFERFADML KRLEKRGVNI TLKHIANSGA ITDLNYAYLD MVRPGITLYG SYPSNDVNKI
     LDLRPAMNFK TKIVYIKEVP ENTSISYGRT FITKRPSKIA TLPIGYADGL NRLLSNNHEV
     LVRGKYVPIV GRVCMDQTMI DVTEVEGVEV GDEVVIFGEQ EGKRITADDI AKKLRTIPHE
     VYCGISRRVP RIYIYRGEVF DVKNYLKI
//
DBGET integrated database retrieval system