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Database: UniProt/TrEMBL
Entry: V5PSE2_9BURK
LinkDB: V5PSE2_9BURK
Original site: V5PSE2_9BURK 
ID   V5PSE2_9BURK            Unreviewed;       375 AA.
AC   V5PSE2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 29.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=U875_13140 {ECO:0000313|EMBL:AHB06203.1};
OS   Pandoraea pnomenusa 3kgm.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=1416914 {ECO:0000313|EMBL:AHB06203.1, ECO:0000313|Proteomes:UP000018768};
RN   [1] {ECO:0000313|EMBL:AHB06203.1, ECO:0000313|Proteomes:UP000018768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3kgm {ECO:0000313|EMBL:AHB06203.1};
RX   PubMed=24812228;
RA   Chan K.G., Yin W.F., Goh S.Y.;
RT   "Complete Genome Sequence of Pandoraea pnomenusa 3kgm, a Quorum-
RT   Sensing Strain Isolated from a Former Landfill Site.";
RL   Genome Announc. 2:e00427-14(2014).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP006900; AHB06203.1; -; Genomic_DNA.
DR   ProteinModelPortal; V5PSE2; -.
DR   EnsemblBacteria; AHB06203; AHB06203; U875_13140.
DR   KEGG; ppk:U875_13140; -.
DR   KO; K01775; -.
DR   BioCyc; PPNO1416914:G13BI-2580-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000018768; 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; 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 {ECO:0000313|Proteomes:UP000018768};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AHB06203.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      251    375       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     54     54       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    272    272       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     320    320       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      54     54       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   375 AA;  40245 MW;  920C44684D464757 CRC64;
     MRYAVGLSRQ ASPPIPFPPM PRPIKVSIHT AALAHNLDVA RRHAPHAKVW AVVKANAYGH
     GIENAYPGLR DADGFGLLDL DEAVRLRELG WAGPILLLEG FFKPEDLAVV DKYGLTTTVH
     CDEQLRMLET TRLTKPLNVQ LKMNSGMNRL GFAPERFRAA WERARAIPGV SQIVLMTHFS
     DADGPRGIAY QMEAFERGAC DVPGERSLAN SAATLFHPGT HGAWVRPGIM LYGSSPKGVD
     VPAAELDLQP TMTLEAELIG TQEVPAGGSV GYGSLFRADA PMRVGTVACG YADGYPRVAP
     TGTPVLVDGV RTRTVGRVSM DMLAVDLTPV PQARVGTPVT LWGRGLSIDE VAASAGTLGY
     ELMCAVTRRV PVHAN
//
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