ALR1_PSEAE
ID ALR1_PSEAE Reviewed; 358 AA.
AC Q9HUN4; Q9S418;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alanine racemase, biosynthetic;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=PA4930;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10977898; DOI=10.1007/s002840010136;
RA Strych U., Huang H.-C., Krause K.L., Benedik M.J.;
RT "Characterization of the alanine racemases from Pseudomonas aeruginosa
RT PAO1.";
RL Curr. Microbiol. 41:290-294(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC Provides the D-alanine required for cell wall biosynthesis.
CC {ECO:0000269|PubMed:10977898}.
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:0000269|PubMed:10977898};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for D-alanine {ECO:0000269|PubMed:10977898};
CC KM=1.1 mM for L-alanine {ECO:0000269|PubMed:10977898};
CC Vmax=40 umol/min/mg enzyme toward D-alanine
CC {ECO:0000269|PubMed:10977898};
CC Vmax=44 umol/min/mg enzyme toward L-alanine
CC {ECO:0000269|PubMed:10977898};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR EMBL; AF165882; AAD47082.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08315.1; -; Genomic_DNA.
DR PIR; D83029; D83029.
DR RefSeq; NP_253617.1; NC_002516.2.
DR RefSeq; WP_003112284.1; NZ_QZGE01000002.1.
DR PDB; 6A2F; X-ray; 2.50 A; A/B=1-358.
DR PDBsum; 6A2F; -.
DR AlphaFoldDB; Q9HUN4; -.
DR SMR; Q9HUN4; -.
DR STRING; 287.DR97_2281; -.
DR PaxDb; Q9HUN4; -.
DR PRIDE; Q9HUN4; -.
DR DNASU; 878646; -.
DR EnsemblBacteria; AAG08315; AAG08315; PA4930.
DR GeneID; 878646; -.
DR KEGG; pae:PA4930; -.
DR PATRIC; fig|208964.12.peg.5163; -.
DR PseudoCAP; PA4930; -.
DR HOGENOM; CLU_028393_1_0_6; -.
DR InParanoid; Q9HUN4; -.
DR OMA; ELMAVQH; -.
DR PhylomeDB; Q9HUN4; -.
DR BioCyc; PAER208964:G1FZ6-5044-MON; -.
DR BRENDA; 5.1.1.1; 5087.
DR SABIO-RK; Q9HUN4; -.
DR UniPathway; UPA00042; UER00497.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008784; F:alanine racemase activity; IDA:PseudoCAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..358
FT /note="Alanine racemase, biosynthetic"
FT /id="PRO_0000114546"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 147
FT /note="S -> N (in Ref. 1; AAD47082)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="I -> L (in Ref. 1; AAD47082)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6A2F"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:6A2F"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:6A2F"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6A2F"
FT TURN 225..229
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 234..246
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:6A2F"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:6A2F"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6A2F"
SQ SEQUENCE 358 AA; 38311 MW; BAA99415A8948BD6 CRC64;
MRPLVATVDL SAIRHNYALA KRCAPQRQAF AVVKANAYGH GAREVVTALH DDADGFAVAC
LEEAAEVRAL HASARILLLE GCFEASEYAL AGQLRLDLVI QGAEQGEAFL AAGLDIPLNV
WLKLDSGMHR LGFDPAALRA WHARLRSHPG VRELNLISHF ACADERNHPL TEQQLESFLG
LLDLDFDQRS LANSAAVLTI PAAHMDWLRP GIMLYGSTPL ADLSAAELGL KPAMSLGAQL
ISLREVAVGE SVGYGATWIA ERPARIGTVS CGYADGYPRT APAGTPVLVG GRRAILAGRV
SMDMLAVDLS DLPEARVGDP VELWGAGLSV DEVARACGTL GYELLSKVTA RVPRRYSH
