ALR1_STAAC
ID ALR1_STAAC Reviewed; 382 AA.
AC Q5HED1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=SACOL2060;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS), AND SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "2.37 Angstrom resolution crystal structure of an alanine racemase (alr)
RT from Staphylococcus aureus subsp. aureus COL.";
RL Submitted (AUG-2010) to the PDB data bank.
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 -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000046; AAW37022.1; -; Genomic_DNA.
DR RefSeq; WP_001281145.1; NC_002951.2.
DR PDB; 3OO2; X-ray; 2.37 A; A/B=1-382.
DR PDBsum; 3OO2; -.
DR AlphaFoldDB; Q5HED1; -.
DR SMR; Q5HED1; -.
DR EnsemblBacteria; AAW37022; AAW37022; SACOL2060.
DR KEGG; sac:SACOL2060; -.
DR HOGENOM; CLU_028393_2_1_9; -.
DR OMA; HMTHFSD; -.
DR UniPathway; UPA00042; UER00497.
DR EvolutionaryTrace; Q5HED1; -.
DR Proteomes; UP000000530; 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..382
FT /note="Alanine racemase 1"
FT /id="PRO_0000114567"
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"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:3OO2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3OO2"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:3OO2"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3OO2"
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
