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Database: UniProt
Entry: B5YIM9
LinkDB: B5YIM9
Original site: B5YIM9 
ID   ALR_THEYD               Reviewed;         363 AA.
AC   B5YIM9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 64.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=THEYE_A0341;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /
OS   YP87).
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae;
OC   Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii
RT   strain ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) 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: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; CP001147; ACI20586.1; -; Genomic_DNA.
DR   RefSeq; WP_012545322.1; NC_011296.1.
DR   RefSeq; YP_002248188.1; NC_011296.1.
DR   ProteinModelPortal; B5YIM9; -.
DR   SMR; B5YIM9; -.
DR   STRING; 289376.THEYE_A0341; -.
DR   EnsemblBacteria; ACI20586; ACI20586; THEYE_A0341.
DR   GeneID; 6941996; -.
DR   KEGG; tye:THEYE_A0341; -.
DR   PATRIC; fig|289376.4.peg.334; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; B5YIM9; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; TYEL289376:G1GCQ-342-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000718; 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    363       Alanine racemase.
FT                                /FTId=PRO_1000213843.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    251    251       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     299    299       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   363 AA;  40664 MW;  3907394BCE8F18C0 CRC64;
     MSRFLQAEIN LKSLIHNFSK IKAHLRNTRV SCKIIAIVKA DAYGHGAVEV ARVFGLLGVD
     YLGVAFSEEA IVLREAGIKV PIIVLFDREI EGVFKYNLIP VIFDYRQAEF LSKEASRRGV
     ILPVHIKVET GMGRLGIYEN PCETIKKIAQ LDNLKIDGVM SHFSRAEDLE WTQEQMKKFS
     KIREFLHNLG MKPLFHIANS QGLNYKEALF DAVRPGLMLY GYGAEGFIPC MTVKTKLLDI
     RKLPKGTPIS YGGTFVTKKD SLIGVIPVGY ADGYFRSLSN KAEVIVRGKR VPVVGTVCMD
     LTMIDLTDIQ EVQIDDEVIL LGKTGSEEIT ASHIAQWAGT IPYEVLTSFG GRARRKYIME
     EEE
//
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