VANT_ENTGA
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 03-AUG-2022, entry version 122.
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., Courvalin P.,
RA Reynolds P.E.;
RT "Characterization and modelling of VanT: a novel, membrane-bound, serine
RT racemase from vancomycin-resistant Enterococcus gallinarum BM4174.";
RL Mol. Microbiol. 31:1653-1664(1999).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RC STRAIN=BM4174;
RX PubMed=10878136; DOI=10.1099/00221287-146-7-1727;
RA Arias C.A., Weisner J., Blackburn J.M., Reynolds P.E.;
RT "Serine and alanine racemase activities of VanT: a protein necessary for
RT vancomycin resistance in Enterococcus gallinarum BM4174.";
RL Microbiology 146:1727-1734(2000).
CC -!- FUNCTION: Catalyzes the interconversion of L-serine and D-serine, and
CC L-alanine and D-alanine. L-alanine is racemized at a rate that is 14%
CC 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, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; 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-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-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 acyltransferase 3
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the alanine racemase
CC family. {ECO:0000305}.
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DR EMBL; AF162694; AAD22403.1; -; Genomic_DNA.
DR RefSeq; WP_003126777.1; NZ_VWOC01000005.1.
DR AlphaFoldDB; Q9X3P3; -.
DR SMR; Q9X3P3; -.
DR PATRIC; fig|1353.6.peg.67; -.
DR BioCyc; MetaCyc:MON-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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:0030378; F:serine racemase activity; IEA:RHEA.
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_dom.
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; Isomerase;
KW Membrane; Peptidoglycan synthesis; Pyridoxal phosphate; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..698
FT /note="Serine/alanine racemase"
FT /id="PRO_0000114606"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..42
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..121
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..183
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..301
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 332..698
FT /note="Racemase"
FT /evidence="ECO:0000305"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 597
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 646
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 371
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="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
