位置:首页 > 蛋白库 > ALR2_PSEAE
ALR2_PSEAE
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   03-AUG-2022, entry version 136.
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 / 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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP   AND LYSINE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-33, AND
RP   CARBOXYLATION 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 and
RT   external aldimine forms.";
RL   Biochemistry 42:14752-14761(2003).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC       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. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   AlphaFoldDB; Q9HTQ2; -.
DR   SMR; Q9HTQ2; -.
DR   STRING; 287.DR97_2673; -.
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   HOGENOM; CLU_028393_1_0_6; -.
DR   InParanoid; Q9HTQ2; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; Q9HTQ2; -.
DR   BioCyc; PAER208964:G1FZ6-5423-MON; -.
DR   BRENDA; 5.1.1.1; 5087.
DR   SABIO-RK; Q9HTQ2; -.
DR   EvolutionaryTrace; Q9HTQ2; -.
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:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Alanine racemase, catabolic"
FT                   /id="PRO_0000114547"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:14674749"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:14674749"
FT   MOD_RES         122
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000269|PubMed:14674749"
FT   CONFLICT        138
FT                   /note="S -> R (in Ref. 1; AAD47081)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="A -> S (in Ref. 1; AAD47081)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="S -> R (in Ref. 1; AAD47081)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           10..24
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           41..48
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           60..68
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           87..92
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           134..146
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          150..156
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           169..181
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           193..198
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           211..214
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          233..245
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          260..269
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          285..288
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          304..307
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          319..327
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           329..335
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   HELIX           340..345
FT                   /evidence="ECO:0007829|PDB:1RCQ"
FT   STRAND          352..355
FT                   /evidence="ECO:0007829|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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024