HYUP_MICLQ
ID HYUP_MICLQ Reviewed; 489 AA.
AC D6R8X8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Hydantoin permease {ECO:0000303|PubMed:16116274};
DE Short=MHP {ECO:0000303|PubMed:16116274};
DE AltName: Full=Hydantoin transport protein {ECO:0000303|PubMed:16621827};
DE AltName: Full=NCS1 benzyl-hydantoin transporter {ECO:0000303|PubMed:18927357};
DE AltName: Full=Nucleobase cation symporter 1 {ECO:0000303|PubMed:24952894};
DE Short=NCS1 {ECO:0000303|PubMed:24952894};
DE AltName: Full=Sodium-coupled secondary active transport protein {ECO:0000303|PubMed:24952894};
DE AltName: Full=Sodium-hydantoin transporter Mhp1 {ECO:0000303|PubMed:24952894};
GN Name=hyuP {ECO:0000303|PubMed:16116274};
OS Microbacterium liquefaciens (Aureobacterium liquefaciens).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX NCBI_TaxID=33918;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AJ 3912;
RX PubMed=16116274; DOI=10.1271/bbb.69.1473;
RA Suzuki S., Takenaka Y., Onishi N., Yokozeki K.;
RT "Molecular cloning and expression of the hyu genes from Microbacterium
RT liquefaciens AJ 3912, responsible for the conversion of 5-substituted
RT hydantoins to alpha-amino acids, in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 69:1473-1482(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=AJ 3912;
RX PubMed=16621827; DOI=10.1128/jb.188.9.3329-3336.2006;
RA Suzuki S., Henderson P.J.;
RT "The hydantoin transport protein from Microbacterium liquefaciens.";
RL J. Bacteriol. 188:3329-3336(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 8-471 IN COMPLEX WITH SODIUM ION,
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=18927357; DOI=10.1126/science.1164440;
RA Weyand S., Shimamura T., Yajima S., Suzuki S., Mirza O., Krusong K.,
RA Carpenter E.P., Rutherford N.G., Hadden J.M., O'Reilly J., Ma P.,
RA Saidijam M., Patching S.G., Hope R.J., Norbertczak H.T., Roach P.C.,
RA Iwata S., Henderson P.J., Cameron A.D.;
RT "Structure and molecular mechanism of a nucleobase-cation-symport-1 family
RT transporter.";
RL Science 322:709-713(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 6-471, AND SUBCELLULAR LOCATION.
RX PubMed=20413494; DOI=10.1126/science.1186303;
RA Shimamura T., Weyand S., Beckstein O., Rutherford N.G., Hadden J.M.,
RA Sharples D., Sansom M.S., Iwata S., Henderson P.J., Cameron A.D.;
RT "Molecular basis of alternating access membrane transport by the sodium-
RT hydantoin transporter Mhp1.";
RL Science 328:470-473(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 11-466 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND SODIUM ION, FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP GLN-42; TRP-117; GLN-121; GLY-219; TRP-220 AND ASN-318.
RX PubMed=24952894; DOI=10.15252/embj.201387557;
RA Simmons K.J., Jackson S.M., Brueckner F., Patching S.G., Beckstein O.,
RA Ivanova E., Geng T., Weyand S., Drew D., Lanigan J., Sharples D.J.,
RA Sansom M.S., Iwata S., Fishwick C.W., Johnson A.P., Cameron A.D.,
RA Henderson P.J.;
RT "Molecular mechanism of ligand recognition by membrane transport protein,
RT Mhp1.";
RL EMBO J. 33:1831-1844(2014).
CC -!- FUNCTION: Nucleobase-proton symporter that mediates the sodium-
CC dependent binding and uptake of 5-aryl-substituted hydantoin compounds
CC (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5-
CC benzyl hydantoin are the preferred substrates, with selectivity for a
CC hydrophobic substituent in position 5 of hydantoin and for the L isomer
CC over the D isomer (PubMed:16621827, PubMed:24952894).
CC {ECO:0000269|PubMed:16621827, ECO:0000269|PubMed:24952894,
CC ECO:0000305|PubMed:16116274}.
CC -!- ACTIVITY REGULATION: Inhibited by dinitrophenol, 5-(2-naphthylmethyl)-
CC D-hydantoin (D-NMH), 5-(2-naphthylmethyl)-L-hydantoin (L-NMH), 5-
CC bromovinylhydantoin (BVH) and 5-indolylmethyl-L-hydantoin (L-IMH)
CC (PubMed:16621827, PubMed:24952894). The affinity of benzyl-hydantoin is
CC increased over 10-fold in the presence of 15 mM of sodium
CC (PubMed:18927357). {ECO:0000269|PubMed:16621827,
CC ECO:0000269|PubMed:18927357, ECO:0000269|PubMed:24952894}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.6. {ECO:0000269|PubMed:16621827};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16621827}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:18927357,
CC ECO:0000305|PubMed:20413494}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR PDB; 2JLN; X-ray; 2.85 A; A=1-488.
DR PDB; 2X79; X-ray; 3.80 A; A=1-488.
DR PDB; 4D1A; X-ray; 3.40 A; A=1-487.
DR PDB; 4D1B; X-ray; 3.80 A; A=1-487.
DR PDB; 4D1C; X-ray; 3.70 A; A=1-487.
DR PDB; 4D1D; X-ray; 3.70 A; A=1-487.
DR PDBsum; 2JLN; -.
DR PDBsum; 2X79; -.
DR PDBsum; 4D1A; -.
DR PDBsum; 4D1B; -.
DR PDBsum; 4D1C; -.
DR PDBsum; 4D1D; -.
DR AlphaFoldDB; D6R8X8; -.
DR SMR; D6R8X8; -.
DR TCDB; 2.A.39.3.6; the nucleobase:cation symporter-1 (ncs1) family.
DR EvolutionaryTrace; D6R8X8; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Metal-binding; Sodium;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Hydantoin permease"
FT /id="PRO_0000439923"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..321
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..424
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..445
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000305|PubMed:18927357,
FT ECO:0000305|PubMed:24952894, ECO:0007744|PDB:2JLN,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 41
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000305|PubMed:18927357,
FT ECO:0000305|PubMed:24952894, ECO:0007744|PDB:2JLN,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24952894,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24952894,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 309
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000305|PubMed:18927357,
FT ECO:0000305|PubMed:24952894, ECO:0007744|PDB:2JLN,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 312
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000305|PubMed:18927357,
FT ECO:0000305|PubMed:24952894, ECO:0007744|PDB:2JLN,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 313
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000305|PubMed:18927357,
FT ECO:0000305|PubMed:24952894, ECO:0007744|PDB:2JLN,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24952894,
FT ECO:0007744|PDB:4D1A, ECO:0007744|PDB:4D1B,
FT ECO:0007744|PDB:4D1C, ECO:0007744|PDB:4D1D"
FT MUTAGEN 42
FT /note="Q->F: Strong decrease in uptake and binding
FT efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 42
FT /note="Q->N: Modest decrease in uptake and binding
FT efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 117
FT /note="W->A: Reduces dramatically the uptake efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 117
FT /note="W->F: Reduces moderately the uptake efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 121
FT /note="Q->N: Partial decrease in efficiency of both binding
FT and uptake."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 219
FT /note="G->I,S: Reduces both binding and uptake efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 220
FT /note="W->A,F: Little effect on uptake efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT MUTAGEN 318
FT /note="N->A: Significant loss of uptake activity and a
FT substantial reduction in binding efficiency."
FT /evidence="ECO:0000269|PubMed:24952894"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4D1A"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 58..79
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 104..137
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 160..190
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 242..278
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 296..311
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 336..349
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:2JLN"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 429..448
FT /evidence="ECO:0007829|PDB:2JLN"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:2JLN"
FT HELIX 462..466
FT /evidence="ECO:0007829|PDB:2JLN"
SQ SEQUENCE 489 AA; 53332 MW; 98796385DB8DB45A CRC64;
MNSTPIEEAR SLLNPSNAPT RYAERSVGPF SLAAIWFAMA IQVAIFIAAG QMTSSFQVWQ
VIVAIAAGCT IAVILLFFTQ SAAIRWGINF TVAARMPFGI RGSLIPITLK ALLSLFWFGF
QTWLGALALD EITRLLTGFT NLPLWIVIFG AIQVVTTFYG ITFIRWMNVF ASPVLLAMGV
YMVYLMLDGA DVSLGEVMSM GGENPGMPFS TAIMIFVGGW IAVVVSIHDI VKECKVDPNA
SREGQTKADA RYATAQWLGM VPASIIFGFI GAASMVLVGE WNPVIAITEV VGGVSIPMAI
LFQVFVLLAT WSTNPAANLL SPAYTLCSTF PRVFTFKTGV IVSAVVGLLM MPWQFAGVLN
TFLNLLASAL GPLAGIMISD YFLVRRRRIS LHDLYRTKGI YTYWRGVNWV ALAVYAVALA
VSFLTPDLMF VTGLIAALLL HIPAMRWVAK TFPLFSEAES RNEDYLRPIG PVAPADESAT
ANTKEQNQR
