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Database: UniProt
Entry: Q9HTQ2
LinkDB: Q9HTQ2
Original site: Q9HTQ2 
ID   ALR2_PSEAE              Reviewed;         357 AA.
AC   Q9HTQ2; Q9S419;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-APR-2019, entry version 124.
DE   RecName: Full=Alanine racemase, catabolic {ECO:0000305|PubMed:10977898};
DE            EC=5.1.1.1 {ECO:0000269|PubMed:10977898};
GN   Name=dadX {ECO:0000303|PubMed:10977898, ECO:0000312|EMBL:AAG08687.1};
GN   OrderedLocusNames=PA5302;
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE AND LYSINE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT
RP   LYS-33, AND CARBAMYLATION AT LYS-122.
RX   PubMed=14674749; DOI=10.1021/bi030165v;
RA   LeMagueres P., Im H., Dvorak A., Strych U., Benedik M.J., Krause K.L.;
RT   "Crystal structure at 1.45 A resolution of alanine racemase from a
RT   pathogenic bacterium, Pseudomonas aeruginosa, contains both internal
RT   and external aldimine forms.";
RL   Biochemistry 42:14752-14761(2003).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to pyruvate by DadA. {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:0000269|PubMed:14674749};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.40 mM for D-alanine {ECO:0000269|PubMed:10977898};
CC         KM=1.40 mM for L-alanine {ECO:0000269|PubMed:10977898};
CC         Vmax=134 umol/min/mg enzyme toward D-alanine
CC         {ECO:0000269|PubMed:10977898};
CC         Vmax=155 umol/min/mg enzyme toward L-alanine
CC         {ECO:0000269|PubMed:10977898};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14674749}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AF165881; AAD47081.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG08687.1; -; Genomic_DNA.
DR   PIR; F82982; F82982.
DR   RefSeq; NP_253989.1; NC_002516.2.
DR   RefSeq; WP_003114351.1; NZ_QZGE01000020.1.
DR   PDB; 1RCQ; X-ray; 1.45 A; A=1-357.
DR   PDBsum; 1RCQ; -.
DR   ProteinModelPortal; Q9HTQ2; -.
DR   SMR; Q9HTQ2; -.
DR   DrugBank; DB03252; D-Lysine.
DR   DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR   PaxDb; Q9HTQ2; -.
DR   PRIDE; Q9HTQ2; -.
DR   EnsemblBacteria; AAG08687; AAG08687; PA5302.
DR   GeneID; 878055; -.
DR   KEGG; pae:PA5302; -.
DR   PATRIC; fig|208964.12.peg.5556; -.
DR   PseudoCAP; PA5302; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   InParanoid; Q9HTQ2; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; Q9HTQ2; -.
DR   BioCyc; PAER208964:G1FZ6-5423-MONOMER; -.
DR   BRENDA; 5.1.1.1; 5087.
DR   SABIO-RK; Q9HTQ2; -.
DR   EvolutionaryTrace; Q9HTQ2; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IDA:PseudoCAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
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; Complete proteome; Isomerase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    357       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114547.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000305|PubMed:14674749}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000269|PubMed:14674749}.
FT   MOD_RES     122    122       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:14674749}.
FT   CONFLICT    138    138       S -> R (in Ref. 1; AAD47081).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       A -> S (in Ref. 1; AAD47081).
FT                                {ECO:0000305}.
FT   CONFLICT    262    262       S -> R (in Ref. 1; AAD47081).
FT                                {ECO:0000305}.
FT   STRAND        5      9       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        10     24       {ECO:0000244|PDB:1RCQ}.
FT   STRAND       26     31       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        33     37       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        41     48       {ECO:0000244|PDB:1RCQ}.
FT   TURN         49     51       {ECO:0000244|PDB:1RCQ}.
FT   STRAND       53     59       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        60     68       {ECO:0000244|PDB:1RCQ}.
FT   STRAND       75     77       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        84     86       {ECO:0000244|PDB:1RCQ}.
FT   HELIX        87     92       {ECO:0000244|PDB:1RCQ}.
FT   STRAND       95     99       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       102    110       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      117    123       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      125    127       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      129    132       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       134    146       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      150    156       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       169    181       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       193    198       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      205    207       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       211    214       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      218    221       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       226    228       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      233    245       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      250    252       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       253    255       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      260    269       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       272    274       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      285    288       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      291    295       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      304    307       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      319    327       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       329    335       {ECO:0000244|PDB:1RCQ}.
FT   HELIX       340    345       {ECO:0000244|PDB:1RCQ}.
FT   STRAND      352    355       {ECO:0000244|PDB:1RCQ}.
SQ   SEQUENCE   357 AA;  38915 MW;  199F4021D02FFF48 CRC64;
     MRPARALIDL QALRHNYRLA REATGARALA VIKADAYGHG AVRCAEALAA EADGFAVACI
     EEGLELREAG IRQPILLLEG FFEASELELI VAHDFWCVVH CAWQLEAIER ASLARPLNVW
     LKMDSGMHRV GFFPEDFSAA HERLRASGKV AKIVMMSHFS RADELDCPRT EEQLAAFAAA
     SQGLEGEISL RNSPAVLGWP KVPSDWVRPG ILLYGATPFE RAHPLADRLR PVMTLESKVI
     SVRDLPAGEP VGYGARYSTE RSQRIGVVAM GYADGYPRHA ADGTLVFIDG KPGRLVGRVS
     MDMLTVDLTD HPQAGLGSRV ELWGPNVPVG ALAAQFGSIP YQLLCNLKRV PRVYSGA
//
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