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Database: UniProt
Entry: Q56346
LinkDB: Q56346
Original site: Q56346 
ID   ALR_TREPA               Reviewed;         377 AA.
AC   Q56346;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 3.
DT   16-JAN-2019, entry version 127.
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=TP_0681;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-198.
RC   STRAIN=Nichols;
RA   Steiner B.M., Rodes B.;
RT   "Partial sequence of alanine racemase from Treponema pallidum.";
RL   Submitted (MAY-1996) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB17466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAC65644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE000520; AAC65644.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U57756; AAB17466.1; ALT_INIT; Genomic_DNA.
DR   PIR; A71295; A71295.
DR   RefSeq; WP_012460586.1; NC_021490.2.
DR   ProteinModelPortal; Q56346; -.
DR   SMR; Q56346; -.
DR   IntAct; Q56346; 1.
DR   STRING; 243276.TP0681; -.
DR   EnsemblBacteria; AAC65644; AAC65644; TP_0681.
DR   GeneID; 34331624; -.
DR   KEGG; tpa:TP_0681; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000811; 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    377       Alanine racemase.
FT                                /FTId=PRO_0000114590.
FT   ACT_SITE     33     33       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     134    134       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      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   377 AA;  40312 MW;  96387BFF1EAD0913 CRC64;
     MACNQALIHL ANLRHNLGEI MSRTRARVCL PVKADAYGHG ACDVAQAALS CGVHSFAVAC
     VQEASQLRAA GVRAPILCLS TPTAEEISSL IEHRVHTVIS ERAHIALIAR ALRQSADTGA
     TCGVHVKIDT GMGRIGCAPD EACALVQMVC ATPGLHLEGV CTHFSVADSV RAEDLQYTEM
     QRAHFMHCVQ YIRKSGISIP LVHAANSAAL LCHPRAHFDM VRPGLLAYGY APESVHPAVR
     SVFLPVMELV TQVRAIKKIP AGAYVSYQRL WRAHTETHVG ILPIGYADGV MRALSPGLQV
     CIGGKWYPVV GAICMDQCVV DLGTPLRVTV GDRVTLFGPQ DAGGPGQGAD VLASHAGTIP
     YELLCAIGKR VERVYIR
//
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