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Database: UniProt
Entry: Q9HUN4
LinkDB: Q9HUN4
Original site: Q9HUN4 
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   05-DEC-2018, entry version 117.
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 /
OS   JCM 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 /
RC   1C / 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 /
RC   1C / 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.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Provides the D-alanine required for cell wall
CC       biosynthesis. {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-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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; NC_002516.2.
DR   PDB; 6A2F; X-ray; 2.50 A; A/B=1-358.
DR   PDBsum; 6A2F; -.
DR   ProteinModelPortal; Q9HUN4; -.
DR   SMR; Q9HUN4; -.
DR   STRING; 208964.PA4930; -.
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   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   InParanoid; Q9HUN4; -.
DR   KO; K01775; -.
DR   OMA; SGAAMYH; -.
DR   PhylomeDB; Q9HUN4; -.
DR   BioCyc; PAER208964:G1FZ6-5044-MONOMER; -.
DR   SABIO-RK; Q9HUN4; -.
DR   UniPathway; UPA00042; UER00497.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002438; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
KW   Complete proteome; Isomerase; Peptidoglycan synthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    358       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114546.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    254    254       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     130    130       Substrate. {ECO:0000250}.
FT   BINDING     302    302       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT    147    147       S -> N (in Ref. 1; AAD47082).
FT                                {ECO:0000305}.
FT   CONFLICT    295    295       I -> L (in Ref. 1; AAD47082).
FT                                {ECO:0000305}.
FT   STRAND        3      8       {ECO:0000244|PDB:6A2F}.
FT   HELIX        10     22       {ECO:0000244|PDB:6A2F}.
FT   STRAND       27     32       {ECO:0000244|PDB:6A2F}.
FT   TURN         36     40       {ECO:0000244|PDB:6A2F}.
FT   HELIX        42     48       {ECO:0000244|PDB:6A2F}.
FT   TURN         49     52       {ECO:0000244|PDB:6A2F}.
FT   STRAND       54     60       {ECO:0000244|PDB:6A2F}.
FT   HELIX        61     70       {ECO:0000244|PDB:6A2F}.
FT   STRAND       72     78       {ECO:0000244|PDB:6A2F}.
FT   HELIX        87     93       {ECO:0000244|PDB:6A2F}.
FT   STRAND       97    100       {ECO:0000244|PDB:6A2F}.
FT   HELIX       103    112       {ECO:0000244|PDB:6A2F}.
FT   STRAND      118    124       {ECO:0000244|PDB:6A2F}.
FT   STRAND      126    128       {ECO:0000244|PDB:6A2F}.
FT   STRAND      130    133       {ECO:0000244|PDB:6A2F}.
FT   HELIX       135    145       {ECO:0000244|PDB:6A2F}.
FT   STRAND      151    157       {ECO:0000244|PDB:6A2F}.
FT   STRAND      165    167       {ECO:0000244|PDB:6A2F}.
FT   HELIX       169    179       {ECO:0000244|PDB:6A2F}.
FT   TURN        180    183       {ECO:0000244|PDB:6A2F}.
FT   HELIX       194    199       {ECO:0000244|PDB:6A2F}.
FT   HELIX       201    203       {ECO:0000244|PDB:6A2F}.
FT   STRAND      206    208       {ECO:0000244|PDB:6A2F}.
FT   HELIX       212    215       {ECO:0000244|PDB:6A2F}.
FT   STRAND      221    223       {ECO:0000244|PDB:6A2F}.
FT   TURN        225    229       {ECO:0000244|PDB:6A2F}.
FT   STRAND      234    246       {ECO:0000244|PDB:6A2F}.
FT   STRAND      251    253       {ECO:0000244|PDB:6A2F}.
FT   HELIX       254    256       {ECO:0000244|PDB:6A2F}.
FT   STRAND      261    270       {ECO:0000244|PDB:6A2F}.
FT   HELIX       273    275       {ECO:0000244|PDB:6A2F}.
FT   STRAND      286    289       {ECO:0000244|PDB:6A2F}.
FT   STRAND      292    296       {ECO:0000244|PDB:6A2F}.
FT   STRAND      305    308       {ECO:0000244|PDB:6A2F}.
FT   STRAND      320    328       {ECO:0000244|PDB:6A2F}.
FT   HELIX       330    336       {ECO:0000244|PDB:6A2F}.
FT   HELIX       341    346       {ECO:0000244|PDB:6A2F}.
FT   STRAND      354    356       {ECO:0000244|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
//
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