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Database: UniProt
Entry: Q8RSU9
LinkDB: Q8RSU9
Original site: Q8RSU9 
ID   ALR_CORGL               Reviewed;         361 AA.
AC   Q8RSU9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   13-FEB-2019, entry version 111.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Cgl0588, cg0681;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12204559; DOI=10.1016/S0168-1656(02)00159-1;
RA   Tauch A., Goetker S., Puehler A., Kalinowski J., Thierbach G.;
RT   "The alanine racemase gene alr is an alternative to antibiotic
RT   resistance genes in cloning systems for industrial Corynebacterium
RT   glutamicum strains.";
RL   J. Biotechnol. 99:79-91(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, COFACTOR, SUBUNIT, AND PYRIDOXAL PHOSPHATE AT LYS-34.
RA   Miyaguchi I., Sasaki C., Kato R., Oikawa T., Sugio S.;
RT   "Crystal structure of alanine racemase from Corynebacterium glutamicum
RT   at 2.1 A resolution.";
RL   Submitted (SEP-2006) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
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:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|Ref.4};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.4}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AY077456; AAL77207.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB97981.1; -; Genomic_DNA.
DR   EMBL; BX927149; CAF19293.1; -; Genomic_DNA.
DR   RefSeq; NP_599824.1; NC_003450.3.
DR   RefSeq; WP_011013748.1; NC_006958.1.
DR   PDB; 2DY3; X-ray; 2.10 A; A/B/C/D=1-361.
DR   PDBsum; 2DY3; -.
DR   ProteinModelPortal; Q8RSU9; -.
DR   SMR; Q8RSU9; -.
DR   STRING; 196627.cg0681; -.
DR   EnsemblBacteria; BAB97981; BAB97981; BAB97981.
DR   EnsemblBacteria; CAF19293; CAF19293; cg0681.
DR   GeneID; 1018592; -.
DR   KEGG; cgb:cg0681; -.
DR   KEGG; cgl:NCgl0563; -.
DR   PATRIC; fig|196627.13.peg.579; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; CORYNE:G18NG-10150-MONOMER; -.
DR   BioCyc; GCF_000196335:G1EEA-596-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   EvolutionaryTrace; Q8RSU9; -.
DR   Proteomes; UP000000582; 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:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isomerase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    361       Alanine racemase.
FT                                /FTId=PRO_0000114512.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     304    304       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT   STRAND        3      9       {ECO:0000244|PDB:2DY3}.
FT   HELIX        10     24       {ECO:0000244|PDB:2DY3}.
FT   STRAND       27     32       {ECO:0000244|PDB:2DY3}.
FT   HELIX        34     39       {ECO:0000244|PDB:2DY3}.
FT   HELIX        42     51       {ECO:0000244|PDB:2DY3}.
FT   STRAND       56     61       {ECO:0000244|PDB:2DY3}.
FT   HELIX        62     70       {ECO:0000244|PDB:2DY3}.
FT   STRAND       75     79       {ECO:0000244|PDB:2DY3}.
FT   HELIX        88     92       {ECO:0000244|PDB:2DY3}.
FT   TURN         93     95       {ECO:0000244|PDB:2DY3}.
FT   STRAND       97    100       {ECO:0000244|PDB:2DY3}.
FT   HELIX       103    110       {ECO:0000244|PDB:2DY3}.
FT   STRAND      117    123       {ECO:0000244|PDB:2DY3}.
FT   STRAND      129    132       {ECO:0000244|PDB:2DY3}.
FT   HELIX       134    145       {ECO:0000244|PDB:2DY3}.
FT   STRAND      150    156       {ECO:0000244|PDB:2DY3}.
FT   HELIX       170    186       {ECO:0000244|PDB:2DY3}.
FT   HELIX       199    204       {ECO:0000244|PDB:2DY3}.
FT   HELIX       206    208       {ECO:0000244|PDB:2DY3}.
FT   HELIX       217    220       {ECO:0000244|PDB:2DY3}.
FT   STRAND      236    241       {ECO:0000244|PDB:2DY3}.
FT   STRAND      244    247       {ECO:0000244|PDB:2DY3}.
FT   STRAND      267    272       {ECO:0000244|PDB:2DY3}.
FT   TURN        275    278       {ECO:0000244|PDB:2DY3}.
FT   HELIX       281    283       {ECO:0000244|PDB:2DY3}.
FT   TURN        284    286       {ECO:0000244|PDB:2DY3}.
FT   STRAND      288    291       {ECO:0000244|PDB:2DY3}.
FT   STRAND      294    300       {ECO:0000244|PDB:2DY3}.
FT   STRAND      307    312       {ECO:0000244|PDB:2DY3}.
FT   STRAND      323    328       {ECO:0000244|PDB:2DY3}.
FT   HELIX       334    340       {ECO:0000244|PDB:2DY3}.
FT   HELIX       345    350       {ECO:0000244|PDB:2DY3}.
FT   STRAND      357    361       {ECO:0000244|PDB:2DY3}.
SQ   SEQUENCE   361 AA;  39174 MW;  6E95CAF6456B6037 CRC64;
     MNLLTTKIDL DAIAHNTRVL KQMAGPAKLM AVVKANAYNH GVEKVAPVIA AHGADAFGVA
     TLAEAMQLRD IGISQEVLCW IWTPEQDFRA AIDRNIDLAV ISPAHAKALI ETDAEHIRVS
     IKIDSGLHRS GVDEQEWEGV FSALAAAPHI EVTGMFTHLA CADEPENPET DRQIIAFRRA
     LALARKHGLE CPVNHVCNSP AFLTRSDLHM EMVRPGLAFY GLEPVAGLEH GLKPAMTWEA
     KVSVVKQIEA GQGTSYGLTW RAEDRGFVAV VPAGYADGMP RHAQGKFSVT IDGLDYPQVG
     RVCMDQFVIS LGDNPHGVEA GAKAVIFGEN GHDATDFAER LDTINYEVVC RPTGRTVRAY
     V
//
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