ALR_STRPN
ID ALR_STRPN Reviewed; 367 AA.
AC P0A2W8; Q54899; Q9S3V7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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; Synonyms=alaR; OrderedLocusNames=SP_1698;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Guynn L.J., Strych U., Benedik M.J.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-367.
RX PubMed=8830261; DOI=10.1046/j.1365-2958.1996.445975.x;
RA Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P.;
RT "The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein
RT involved in DNA repair and in three-strand recombination.";
RL Mol. Microbiol. 19:1035-1045(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-40, AND CARBOXYLATION AT
RP LYS-129.
RX PubMed=21612658; DOI=10.1186/1471-2180-11-116;
RA Im H., Sharpe M.L., Strych U., Davlieva M., Krause K.L.;
RT "The crystal structure of alanine racemase from Streptococcus pneumoniae, a
RT target for structure-based drug design.";
RL BMC Microbiol. 11:116-116(2011).
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 ECO:0000269|PubMed:21612658};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21612658}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AF171873; AAD51027.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75776.1; -; Genomic_DNA.
DR EMBL; Z49988; CAA90279.1; -; Genomic_DNA.
DR PIR; G95197; G95197.
DR PIR; S71015; S71015.
DR RefSeq; WP_000648075.1; NZ_AKVY01000001.1.
DR PDB; 3S46; X-ray; 2.00 A; A/B=1-367.
DR PDBsum; 3S46; -.
DR AlphaFoldDB; P0A2W8; -.
DR SMR; P0A2W8; -.
DR STRING; 170187.SP_1698; -.
DR EnsemblBacteria; AAK75776; AAK75776; SP_1698.
DR GeneID; 60232913; -.
DR KEGG; spn:SP_1698; -.
DR eggNOG; COG0787; Bacteria.
DR OMA; WEILCGF; -.
DR PhylomeDB; P0A2W8; -.
DR BioCyc; SPNE170187:G1FZB-1721-MON; -.
DR BRENDA; 5.1.1.1; 1960.
DR UniPathway; UPA00042; UER00497.
DR EvolutionaryTrace; P0A2W8; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate.
FT CHAIN 1..367
FT /note="Alanine racemase"
FT /id="PRO_0000114581"
FT ACT_SITE 40
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 263
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 129
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:21612658"
FT CONFLICT 354
FT /note="V -> E (in Ref. 3; CAA90279)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3S46"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3S46"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:3S46"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:3S46"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:3S46"
SQ SEQUENCE 367 AA; 39858 MW; A79E2F1B439B18B7 CRC64;
MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA VAKAIQDDVD
GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD FTLTVAGLEW IQALLDKEVD
LTGLTVHLKI DSGMGRIGFR EASEVEQAQD LLQQHGVCVE GIFTHFATAD EESDDYFNAQ
LERFKTILAS MKEVPELVHA SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI
PALTLESALV HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ
ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI NYEVVCLLSD
RIPREYY
