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Database: UniProt
Entry: Q9KSE5
LinkDB: Q9KSE5
Original site: Q9KSE5 
ID   ALR2_VIBCH              Reviewed;         392 AA.
AC   Q9KSE5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   10-APR-2019, entry version 106.
DE   RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr2; OrderedLocusNames=VC_1312;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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};
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   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF94470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE003852; AAF94470.1; ALT_INIT; Genomic_DNA.
DR   PIR; A82215; A82215.
DR   PDB; 4BEQ; X-ray; 1.50 A; A=9-392.
DR   PDB; 4BEU; X-ray; 1.15 A; A=9-392.
DR   PDBsum; 4BEQ; -.
DR   PDBsum; 4BEU; -.
DR   ProteinModelPortal; Q9KSE5; -.
DR   SMR; Q9KSE5; -.
DR   STRING; 243277.VC_1312; -.
DR   DNASU; 2614766; -.
DR   EnsemblBacteria; AAF94470; AAF94470; VC_1312.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   OMA; NTVMVDV; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008784; F:alanine racemase activity; ISS:TIGR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; ISS:TIGR.
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    392       Alanine racemase 2.
FT                                /FTId=PRO_0000114592.
FT   ACT_SITE     59     59       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    284    284       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     158    158       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     332    332       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      59     59       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   HELIX        20     24       {ECO:0000244|PDB:4BEU}.
FT   STRAND       26     33       {ECO:0000244|PDB:4BEU}.
FT   HELIX        34     45       {ECO:0000244|PDB:4BEU}.
FT   STRAND       54     57       {ECO:0000244|PDB:4BEU}.
FT   HELIX        59     63       {ECO:0000244|PDB:4BEU}.
FT   HELIX        67     76       {ECO:0000244|PDB:4BEU}.
FT   STRAND       81     86       {ECO:0000244|PDB:4BEU}.
FT   HELIX        87     95       {ECO:0000244|PDB:4BEU}.
FT   STRAND      100    104       {ECO:0000244|PDB:4BEU}.
FT   HELIX       110    115       {ECO:0000244|PDB:4BEU}.
FT   HELIX       117    119       {ECO:0000244|PDB:4BEU}.
FT   STRAND      122    125       {ECO:0000244|PDB:4BEU}.
FT   HELIX       128    141       {ECO:0000244|PDB:4BEU}.
FT   STRAND      145    151       {ECO:0000244|PDB:4BEU}.
FT   STRAND      158    161       {ECO:0000244|PDB:4BEU}.
FT   HELIX       166    176       {ECO:0000244|PDB:4BEU}.
FT   STRAND      181    187       {ECO:0000244|PDB:4BEU}.
FT   HELIX       195    215       {ECO:0000244|PDB:4BEU}.
FT   HELIX       220    222       {ECO:0000244|PDB:4BEU}.
FT   STRAND      224    228       {ECO:0000244|PDB:4BEU}.
FT   HELIX       230    235       {ECO:0000244|PDB:4BEU}.
FT   HELIX       237    239       {ECO:0000244|PDB:4BEU}.
FT   TURN        248    252       {ECO:0000244|PDB:4BEU}.
FT   STRAND      264    269       {ECO:0000244|PDB:4BEU}.
FT   STRAND      272    276       {ECO:0000244|PDB:4BEU}.
FT   STRAND      281    283       {ECO:0000244|PDB:4BEU}.
FT   HELIX       284    286       {ECO:0000244|PDB:4BEU}.
FT   STRAND      294    300       {ECO:0000244|PDB:4BEU}.
FT   HELIX       303    305       {ECO:0000244|PDB:4BEU}.
FT   HELIX       309    311       {ECO:0000244|PDB:4BEU}.
FT   TURN        312    314       {ECO:0000244|PDB:4BEU}.
FT   STRAND      316    319       {ECO:0000244|PDB:4BEU}.
FT   STRAND      322    326       {ECO:0000244|PDB:4BEU}.
FT   STRAND      335    338       {ECO:0000244|PDB:4BEU}.
FT   STRAND      350    357       {ECO:0000244|PDB:4BEU}.
FT   HELIX       364    371       {ECO:0000244|PDB:4BEU}.
FT   HELIX       375    385       {ECO:0000244|PDB:4BEU}.
FT   STRAND      388    391       {ECO:0000244|PDB:4BEU}.
SQ   SEQUENCE   392 AA;  42498 MW;  C0211DC2661691FD CRC64;
     MPSFSLSAAP LHIDTALPDA AQIQQSNSWL EISLGQFQSN IEQFKSHMNA NTKICAIMKA
     DAYGNGIRGL MPTIIAQGIP CVGVASNAEA RAVRESGFKG ELIRVRSASL SEMSSALDLN
     IEELIGTHQQ ALDLAELAKQ SGKTLKVHIA LNDGGMGRNG IDMTTEAGKK EAVSIATQPS
     LSVVGIMTHF PNYNADEVRA KLAQFKESST WLMQQANLKR EEITLHVANS YTALNVPEAQ
     LDMVRPGGVL FGDLPTNPEY PSIVSFKTRV SSLHHLPKDS TVGYDSTFTT SRDSVLANLP
     VGYSDGYPRK MGNKAEVLIN GQRAKVVGVT SMNTTVVDVT EIKGVLPGQE VVLFGQQQKQ
     SIAVSEMENN AELIFPELYT LWGTSNPRFY VK
//
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