ALR_TREPA
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 03-AUG-2022, entry version 138.
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; Treponemataceae; 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., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis 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-alanine. May
CC also act on other amino acids. {ECO:0000255|HAMAP-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-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC 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};
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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 AlphaFoldDB; Q56346; -.
DR SMR; Q56346; -.
DR IntAct; Q56346; 1.
DR STRING; 243276.TPANIC_0681; -.
DR EnsemblBacteria; AAC65644; AAC65644; TP_0681.
DR GeneID; 57879206; -.
DR KEGG; tpa:TP_0681; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_12; -.
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 Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..377
FT /note="Alanine racemase"
FT /id="PRO_0000114590"
FT ACT_SITE 33
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 267
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 33
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="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
