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Database: UniProt
Entry: Q8D6Q0
LinkDB: Q8D6Q0
Original site: Q8D6Q0 
ID   ALR2_VIBVU              Reviewed;         408 AA.
AC   Q8D6Q0;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   13-FEB-2019, entry version 103.
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=VV2_0478;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H.,
RA   Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; AE016796; AAO07429.1; -; Genomic_DNA.
DR   RefSeq; WP_011081429.1; NC_004460.2.
DR   ProteinModelPortal; Q8D6Q0; -.
DR   SMR; Q8D6Q0; -.
DR   EnsemblBacteria; AAO07429; AAO07429; VV2_0478.
DR   KEGG; vvu:VV2_0478; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000279190; -.
DR   KO; K01775; -.
DR   OMA; NTVMVDV; -.
DR   BioCyc; VVUL216895:G1GJ4-3687-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002275; Chromosome 2.
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; 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   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    408       Alanine racemase 2.
FT                                /FTId=PRO_0000114596.
FT   ACT_SITE     75     75       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    300    300       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     174    174       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     348    348       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      75     75       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   408 AA;  44106 MW;  3D8A964B40B670F4 CRC64;
     MNFKKTLLSI AIASASLTPA FSYSAPLLLD NTVHQTSQIA GANAWLEISL GQFKSNIEQF
     KSHIAPQTKI CAVMKADAYG NGIRGLMPTI LEQQIPCVAI ASNAEAKLVR ESGFEGELIR
     VRSASTSEIE QALSLDIEEL IGSEQQAREL ASLAEKYSKT IKVHLALNDG GMGRNGIDMS
     TERGPKEAVA IATHPSVAVV GIMTHFPNYN AEDVRTKLKS FNQHAQWLME SAGLKREEIT
     LHVANSYTAL NVPEAQLDMV RPGGVLYGDL PTNPEYPSIV AFKTRVASLH SLPAGSTVGY
     DSTFTTANDA VMANLTVGYS DGYPRKMGNK AQVLINGQRA NVVGVASMNT TMVDVSNIKG
     VLPGDEVTLF GAQKNQHISV GEMEENAEVI FPELYTIWGT SNPRFYVK
//
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