ID ALR_BACST STANDARD; PRT; 388 AA. AC P10724; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-MAY-2006, entry version 63. DE Alanine racemase (EC 5.1.1.1). GN Name=alr; Synonyms=dal; OS Bacillus stearothermophilus (Geobacillus stearothermophilus). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88209488; PubMed=2835089; RA Tanizawa K., Ohshima A., Scheidegger A., Inagaki K., Tanaka H., RA Soda K.; RT "Thermostable alanine racemase from Bacillus stearothermophilus: DNA RT and protein sequence determination and secondary structure RT prediction."; RL Biochemistry 27:1311-1316(1988). RN [2] RP PROTEIN SEQUENCE OF 31-43. RX MEDLINE=89229030; PubMed=2496744; RA Faraci W.S., Walsh C.T.; RT "Mechanism of inactivation of alanine racemase by beta, beta, beta- RT trifluoroalanine."; RL Biochemistry 28:431-437(1989). RN [3] RP PROTEIN SEQUENCE OF 36-43. RX MEDLINE=86269909; PubMed=3730360; RA Badet B., Inagaki K., Soda K., Walsh C.T.; RT "Time-dependent inhibition of Bacillus stearothermophilus alanine RT racemase by (1-aminoethyl)phosphonate isomers by isomerization to RT noncovalent slowly dissociating enzyme-(1-aminoethyl)phosphonate RT complexes."; RL Biochemistry 25:3275-3282(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SEQUENCE REVISION. RX MEDLINE=97178818; PubMed=9063881; DOI=10.1021/bi961856c; RA Shaw J.P., Petsko G.A., Ringe D.; RT "Determination of the structure of alanine racemase from Bacillus RT stearothermophilus at 1.9-A resolution."; RL Biochemistry 36:1329-1342(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX MEDLINE=98337786; PubMed=9671513; DOI=10.1021/bi980692s; RA Stamper C.G., Morollo A.A., Ringe D.; RT "Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a RT stable external aldimine."; RL Biochemistry 37:10438-10445(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RC STRAIN=IFO 12550; RX MEDLINE=99178834; PubMed=10079072; DOI=10.1021/bi9822729; RA Morollo A.A., Petsko G.A., Ringe D.; RT "Structure of a Michaelis complex analogue: propionate binds in the RT substrate carboxylate site of alanine racemase."; RL Biochemistry 38:3293-3301(1999). RN [7] RP MUTAGENESIS OF ARG-219. RX MEDLINE=99212226; PubMed=10194319; DOI=10.1021/bi982924t; RA Sun S., Toney M.D.; RT "Evidence for a two-base mechanism involving tyrosine-265 from RT arginine-219 mutants of alanine racemase."; RL Biochemistry 38:4058-4065(1999). RN [8] RP ACTIVE SITES, AND MUTAGENESIS. RX MEDLINE=99434146; PubMed=10502689; RA Watanabe A., Yoshimura T., Mikami B., Esaki N.; RT "Tyrosine 265 of alanine racemase serves as a base abstracting alpha- RT hydrogen from L-alanine: the counterpart residue to lysine 39 specific RT to D-alanine."; RL J. Biochem. 126:781-786(1999). CC -!- FUNCTION: Provides the D-alanine required for cell wall CC biosynthesis. CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: D-alanine branch of peptidoglycan biosynthesis; first CC step. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the alanine racemase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M19142; AAA22220.1; -; Genomic_DNA. DR PIR; A29984; A29984. DR PDB; 1BD0; X-ray; A/B=1-388. DR PDB; 1EPV; X-ray; A/B=2-388. DR PDB; 1FTX; X-ray; A/B=2-388. DR PDB; 1L6F; X-ray; A/B=1-388. DR PDB; 1L6G; X-ray; A/B=1-388. DR PDB; 1NIU; X-ray; A/B=1-388. DR PDB; 1SFT; X-ray; A/B=1-388. DR PDB; 1XQK; X-ray; A/B=1-388. DR PDB; 1XQL; X-ray; A/B=1-388. DR PDB; 2SFP; X-ray; A/B=1-388. DR LinkHub; P10724; -. DR HAMAP; MF_01201; -; 1. DR InterPro; IPR012155; Ala_racemase. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR000821; Ala_racemase_reg. DR InterPro; IPR009006; Racem_decarbox_C. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF001401; Ala_racemase; 1. DR PRINTS; PR00992; ALARACEMASE. DR TIGRFAMs; TIGR00492; alr; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. KW 3D-structure; Cell shape; Cell wall; Direct protein sequencing; KW Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate. FT CHAIN 1 388 Alanine racemase. FT /FTId=PRO_0000114499. FT ACT_SITE 39 39 Proton acceptor; specific for D-alanine. FT ACT_SITE 265 265 Proton acceptor; specific for L-alanine. FT BINDING 39 39 Pyridoxal phosphate (covalent). FT MUTAGEN 39 39 K->A: Loss of activity. FT MUTAGEN 166 166 H->A: 6.5-fold decrease in activity. FT MUTAGEN 219 219 R->A: 100-fold decrease in activity. FT MUTAGEN 219 219 R->E: 1000-fold decrease in activity. FT MUTAGEN 219 219 R->K: 4-fold decrease in activity. FT MUTAGEN 265 265 Y->A: 5000-fold decrease in activity. FT MUTAGEN 265 265 Y->F: Loss of activity. FT MUTAGEN 265 265 Y->S: 2000-fold decrease in activity. FT CONFLICT 37 38 VV -> PP (in Ref. 3). FT CONFLICT 57 62 AGASRL -> RGPPP (in Ref. 1). FT CONFLICT 288 289 WL -> V (in Ref. 1). FT STRAND 6 13 FT HELIX 14 27 FT STRAND 28 28 FT TURN 30 31 FT STRAND 33 37 FT HELIX 39 43 FT TURN 44 45 FT HELIX 47 57 FT TURN 58 58 FT STRAND 61 66 FT HELIX 67 75 FT TURN 76 77 FT STRAND 80 80 FT STRAND 82 84 FT STRAND 86 86 FT HELIX 90 98 FT TURN 99 100 FT STRAND 101 105 FT HELIX 108 117 FT STRAND 121 122 FT STRAND 124 130 FT STRAND 132 134 FT STRAND 136 139 FT STRAND 141 141 FT HELIX 142 154 FT STRAND 155 155 FT TURN 156 157 FT STRAND 158 164 FT STRAND 168 169 FT TURN 170 171 FT STRAND 172 173 FT HELIX 176 189 FT TURN 190 191 FT STRAND 193 194 FT STRAND 197 200 FT HELIX 204 209 FT TURN 211 212 FT STRAND 213 213 FT TURN 215 216 FT STRAND 217 220 FT HELIX 222 225 FT TURN 226 226 FT STRAND 229 229 FT HELIX 231 236 FT STRAND 238 239 FT STRAND 245 250 FT STRAND 252 257 FT TURN 259 260 FT STRAND 262 264 FT HELIX 265 267 FT STRAND 269 270 FT STRAND 273 281 FT HELIX 284 286 FT TURN 287 287 FT HELIX 290 294 FT STRAND 296 299 FT TURN 300 301 FT STRAND 302 308 FT STRAND 312 313 FT STRAND 315 318 FT STRAND 320 321 FT TURN 325 326 FT STRAND 328 335 FT TURN 336 337 FT STRAND 338 340 FT HELIX 342 349 FT TURN 350 350 FT STRAND 351 351 FT TURN 353 354 FT HELIX 355 359 FT STRAND 360 360 FT TURN 362 363 FT STRAND 364 364 FT STRAND 366 370 FT TURN 371 372 FT STRAND 373 378 FT TURN 380 381 SQ SEQUENCE 388 AA; 43593 MW; F54AA581F135EA7A CRC64; MNDFHRDTWA EVDLDAIYDN VENLRRLLPD DTHIMAVVKA NAYGHGDVQV ARTALEAGAS RLAVAFLDEA LALREKGIEA PILVLGASRP ADAALAAQQR IALTVFRSDW LEEASALYSG PFPIHFHLKM DTGMGRLGVK DEEETKRIVA LIERHPHFVL EGLYTHFATA DEVNTDYFSY QYTRFLHMLE WLPSRPPLVH CANSAASLRF PDRTFNMVRF GIAMYGLAPS PGIKPLLPYP LKEAFSLHSR LVHVKKLQPG EKVSYGATYT AQTEEWIGTI PIGYADGWLR RLQHFHVLVD GQKAPIVGRI CMDQCMIRLP GPLPVGTKVT LIGRQGDEVI SIDDVARHLE TINYEVPCTI SYRVPRIFFR HKRIMEVRNA IGRGESSA //