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Database: UniProt
Entry: Q9X3P3
LinkDB: Q9X3P3
Original site: Q9X3P3 
ID   VANT_ENTGA              Reviewed;         698 AA.
AC   Q9X3P3;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   05-DEC-2018, entry version 112.
DE   RecName: Full=Serine/alanine racemase {ECO:0000305|PubMed:10878136};
DE            EC=5.1.1.- {ECO:0000269|PubMed:10209740, ECO:0000269|PubMed:10878136};
DE            EC=5.1.1.1 {ECO:0000269|PubMed:10878136};
DE   AltName: Full=Vancomycin C-type resistance protein VanT;
GN   Name=vanT {ECO:0000303|PubMed:10209740, ECO:0000303|PubMed:10878136};
OS   Enterococcus gallinarum.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RC   STRAIN=BM4174;
RX   PubMed=10209740; DOI=10.1046/j.1365-2958.1999.01294.x;
RA   Arias C.A., Martin-Martinez M., Blundell T.L., Arthur M.,
RA   Courvalin P., Reynolds P.E.;
RT   "Characterization and modelling of VanT: a novel, membrane-bound,
RT   serine racemase from vancomycin-resistant Enterococcus gallinarum
RT   BM4174.";
RL   Mol. Microbiol. 31:1653-1664(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND DOMAIN.
RC   STRAIN=BM4174;
RX   PubMed=10878136;
RA   Arias C.A., Weisner J., Blackburn J.M., Reynolds P.E.;
RT   "Serine and alanine racemase activities of VanT: a protein necessary
RT   for vancomycin resistance in Enterococcus gallinarum BM4174.";
RL   Microbiology 146:1727-1734(2000).
CC   -!- FUNCTION: Catalyzes the interconversion of L-serine and D-serine,
CC       and L-alanine and D-alanine. L-alanine is racemized at a rate that
CC       is 14% of that of L-serine. Necessary for vancomycin resistance in
CC       E.gallinarum. {ECO:0000269|PubMed:10209740,
CC       ECO:0000269|PubMed:10878136}.
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:10878136};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:35247;
CC         Evidence={ECO:0000269|PubMed:10209740,
CC         ECO:0000269|PubMed:10878136};
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   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:10209740}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10209740,
CC       ECO:0000269|PubMed:10878136}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10209740, ECO:0000269|PubMed:10878136}.
CC   -!- DOMAIN: The cytoplasmic C-terminal domain is responsible for the
CC       racemase activity. {ECO:0000269|PubMed:10878136}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       acyltransferase 3 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the alanine
CC       racemase family. {ECO:0000305}.
DR   EMBL; AF162694; AAD22403.1; -; Genomic_DNA.
DR   RefSeq; WP_003126777.1; NZ_JMGP01000002.1.
DR   ProteinModelPortal; Q9X3P3; -.
DR   SMR; Q9X3P3; -.
DR   PATRIC; fig|1353.6.peg.67; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   BioCyc; MetaCyc:MONOMER-15476; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR002656; Acyl_transf_3.
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   InterPro; IPR011248; Serine/alanine_racemase.
DR   Pfam; PF01757; Acyl_transf_3; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF036464; Ser_ala_racem; 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   Antibiotic resistance; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Isomerase; Membrane; Peptidoglycan synthesis; Pyridoxal phosphate;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    698       Serine/alanine racemase.
FT                                /FTId=PRO_0000114606.
FT   TOPO_DOM      1     10       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM     11     31       Helical. {ECO:0000255}.
FT   TOPO_DOM     32     42       Extracellular. {ECO:0000305}.
FT   TRANSMEM     43     63       Helical. {ECO:0000255}.
FT   TOPO_DOM     64     81       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM     82    102       Helical. {ECO:0000255}.
FT   TOPO_DOM    103    121       Extracellular. {ECO:0000305}.
FT   TRANSMEM    122    142       Helical. {ECO:0000255}.
FT   TOPO_DOM    143    147       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    148    168       Helical. {ECO:0000255}.
FT   TOPO_DOM    169    183       Extracellular. {ECO:0000305}.
FT   TRANSMEM    184    204       Helical. {ECO:0000255}.
FT   TOPO_DOM    205    216       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    217    237       Helical. {ECO:0000255}.
FT   TOPO_DOM    238    244       Extracellular. {ECO:0000305}.
FT   TRANSMEM    245    265       Helical. {ECO:0000255}.
FT   TOPO_DOM    266    274       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    275    295       Helical. {ECO:0000255}.
FT   TOPO_DOM    296    301       Extracellular. {ECO:0000305}.
FT   TRANSMEM    302    322       Helical. {ECO:0000255}.
FT   TOPO_DOM    323    698       Cytoplasmic. {ECO:0000305}.
FT   REGION      332    698       Racemase. {ECO:0000305}.
FT   ACT_SITE    371    371       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   ACT_SITE    597    597       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     465    465       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     646    646       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES     371    371       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   698 AA;  78587 MW;  59998EA3E4778636 CRC64;
     MKNKGIDQFR VIAAMMVVAI HCLPLHYLWP EGDILITLTI FRVAVPFFFM ISGYYVFAEL
     AVANSYPSRQ RVFNFIKKQL KVYLLATLMF LPLALYSQTI GFDLPVGTLV QVLLVNGILY
     HLWYFPALIT GSLLLTSLLI HVSFKKVFWL AAGLYLIGLG GDSWFGLIQQ TPIEPFYTAV
     FHLLDGTRNG IFFTPLFLCL GVLVRKQSEK RSLSKTALFF LISLIGLLIE SAYLHGFSIP
     KHDSMYLFLP VVLFFLFPLI LRWHPHRTWK HPGQLSLWLY LLHPYTIAGT HFLSQKISIL
     QNNLINYLVV LILTIGFICL FLRQKHSWFR HKQTTPVKRA VKEFSKTALL HNLQEIQRII
     SPKTKVMAVV KADAYGCGAK EVAPVLEQAG IDFFAVATID EGIRLRKNAV KSPILVLGYT
     SPKRIKELRR YSLTQSIISE GHAVALSQRK VAIDCHLAID TGMHRLGVTP TIDSILSIFD
     LPFLTISGVY SHLGSADRLN PDSMIRTQKQ IACFDQILLE LDQRQISYGI THLQSSYGIL
     NYPDLNYDYV RPGILLTGSL SDTNEPTKQR VSLQPILTLK AQLITKRVVA KGEAIGYGQT
     AVANQETTVG VVSIGYCDGL PRSLSNQEFC LSYRGQSLPQ IGLICMDMLL IDLSHCPTIP
     IESEIEILTD WSDTAEQVQT ITNELICRIG PRVSARIK
//
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