ID ALR1_STAA8 Reviewed; 382 AA.
AC Q9ZAH5; Q2FWI6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr1; Synonyms=alr; OrderedLocusNames=SAOUHSC_02305;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9756984; DOI=10.1016/s0378-1119(98)00404-1;
RA Kullik I., Jenni R., Berger-Baechi B.;
RT "Sequence of the putative alanine racemase operon in Staphylococcus aureus:
RT insertional interruption of this operon reduces D-alanine substitution of
RT lipoteichoic acid and autolysis.";
RL Gene 219:9-17(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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}.
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DR EMBL; Y16431; CAA76221.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31339.1; -; Genomic_DNA.
DR RefSeq; WP_001281145.1; NZ_LS483365.1.
DR RefSeq; YP_500784.1; NC_007795.1.
DR AlphaFoldDB; Q9ZAH5; -.
DR SMR; Q9ZAH5; -.
DR STRING; 93061.SAOUHSC_02305; -.
DR PaxDb; 1280-SAXN108_2315; -.
DR GeneID; 3920930; -.
DR KEGG; sao:SAOUHSC_02305; -.
DR PATRIC; fig|93061.5.peg.2089; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_1_9; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR PRO; PR:Q9ZAH5; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..382
FT /note="Alanine racemase 1"
FT /id="PRO_0000114573"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 382 AA; 42823 MW; 52B3C88E9811956D CRC64;
MSDKYYRSAY MNVDLNAVAS NFKVFSTLHP NKTVMAVVKA NAYGLGSVKV ARHLMENGAT
FFAVATLDEA IELRMHGITA KILVLGVLPA KDIDKAIQHR VALTVPSKQW LKEAIKNISG
EQEKKLWLHI KLDTGMGRLG IKDTKTYQEV IEIIQQYEQL VFEGVFTHFA CADEPGDMTT
EQYQRFKDMV NEAIKPEYIH CQNSAGSLLM DCQFCNAIRP GISLYGYYPS EYVQQKVKVH
LKPSVQLIAN VVQTKTLQAG ESVSYGATYT ATDPTTIALL PIGYADGYLR IMQGSFVNVN
GHQCEVIGRV CMDQTIVKVP DQVKAGDSVI LIDNHRESPQ SVEVVAEKQH TINYEVLCNL
SRRLPRIYHD GDQRFVTNEL LK
//
