ALR1_STAAM
ID ALR1_STAAM Reviewed; 382 AA.
AC P63479; Q99SI5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SAV2070;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND ACETATE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, SUBUNIT, ACTIVE SITE, PYRIDOXAL PHOSPHATE AT LYS-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=22194336; DOI=10.1107/s0907444911050682;
RA Scaletti E.R., Luckner S.R., Krause K.L.;
RT "Structural features and kinetic characterization of alanine racemase from
RT Staphylococcus aureus (Mu50).";
RL Acta Crystallogr. D 68:82-92(2012).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC {ECO:0000269|PubMed:22194336}.
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 ECO:0000269|PubMed:22194336};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201,
CC ECO:0000269|PubMed:22194336};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.89 mM for D-alanine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22194336};
CC KM=2.77 mM for L-alanine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22194336};
CC Vmax=91 umol/min/mg enzyme toward D-alanine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22194336};
CC Vmax=250 umol/min/mg enzyme toward L-alanine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22194336};
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:22194336}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; BA000017; BAB58232.1; -; Genomic_DNA.
DR RefSeq; WP_001281154.1; NC_002758.2.
DR PDB; 4A3Q; X-ray; 2.15 A; A/B=1-382.
DR PDB; 6G56; X-ray; 2.15 A; A/B=2-382.
DR PDB; 6G58; X-ray; 1.90 A; A/B=2-382.
DR PDB; 6G59; X-ray; 2.45 A; A/B=2-382.
DR PDBsum; 4A3Q; -.
DR PDBsum; 6G56; -.
DR PDBsum; 6G58; -.
DR PDBsum; 6G59; -.
DR AlphaFoldDB; P63479; -.
DR SMR; P63479; -.
DR World-2DPAGE; 0002:P63479; -.
DR PaxDb; P63479; -.
DR EnsemblBacteria; BAB58232; BAB58232; SAV2070.
DR KEGG; sav:SAV2070; -.
DR HOGENOM; CLU_028393_2_1_9; -.
DR OMA; HMTHFSD; -.
DR PhylomeDB; P63479; -.
DR BioCyc; SAUR158878:SAV_RS11330-MON; -.
DR BRENDA; 5.1.1.1; 3352.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000002481; 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_0000114568"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000305|PubMed:22194336"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000305|PubMed:22194336"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6G59"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6G58"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6G58"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6G58"
SQ SEQUENCE 382 AA; 42809 MW; A46B7E55F5A65E41 CRC64;
MSDKYYRSAY MNVDLNAVAS NFKVFSTLHP NKTVMAVVKA NAYGLGSVKV ARHLMENGAT
FFAVATLDEA IELRMHGITA KILVLGVLPA KDIDKAIQHR VALTVPSKQW LKEAIKNISG
EQEKKLWLHI KLDTGMGRLG IKDTNTYQEV IEIIQQYEQL VFEGVFTHFA CADEPGDMTT
EQYQRFKDMV NEAIKPEYIH CQNSAGSLLM DCQFCNAIRP GISLYGYYPS EYVQQKVKVH
LKPSVQLIAN VVQTKTLQAG ESVSYGATYT ATDPTTIALL PIGYADGYLR IMQGSFVNVN
GHQCEVIGRV CMDQTIVKVP DQVKAGDSVI LIDNHRESPQ SVEVVAEKQH TINYEVLCNL
SRRLPRIYHD GDQRFVTNEL LK
