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Hydantoin permease (MHP) (Hydantoin transport protein) (NCS1 benzyl-hydantoin transporter) (Nucleobase cation symporter 1) (NCS1) (Sodium-coupled secondary active transport protein) (Sodium-hydantoin transporter Mhp1)

 HYUP_MICLQ              Reviewed;         489 AA.
D6R8X8;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 2.
30-AUG-2017, entry version 31.
RecName: Full=Hydantoin permease {ECO:0000303|PubMed:16116274};
Short=MHP {ECO:0000303|PubMed:16116274};
AltName: Full=Hydantoin transport protein {ECO:0000303|PubMed:16621827};
AltName: Full=NCS1 benzyl-hydantoin transporter {ECO:0000303|PubMed:18927357};
AltName: Full=Nucleobase cation symporter 1 {ECO:0000303|PubMed:24952894};
Short=NCS1 {ECO:0000303|PubMed:24952894};
AltName: Full=Sodium-coupled secondary active transport protein {ECO:0000303|PubMed:24952894};
AltName: Full=Sodium-hydantoin transporter Mhp1 {ECO:0000303|PubMed:24952894};
Name=hyuP {ECO:0000303|PubMed:16116274};
Microbacterium liquefaciens (Aureobacterium liquefaciens).
Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
Microbacterium.
NCBI_TaxID=33918;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=AJ 3912;
PubMed=16116274;
Suzuki S., Takenaka Y., Onishi N., Yokozeki K.;
"Molecular cloning and expression of the hyu genes from Microbacterium
liquefaciens AJ 3912, responsible for the conversion of 5-substituted
hydantoins to alpha-amino acids, in Escherichia coli.";
Biosci. Biotechnol. Biochem. 69:1473-1482(2005).
[2]
PROTEIN SEQUENCE OF 1-10, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
ENZYME REGULATION, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
STRAIN=AJ 3912;
PubMed=16621827; DOI=10.1128/JB.188.9.3329-3336.2006;
Suzuki S., Henderson P.J.;
"The hydantoin transport protein from Microbacterium liquefaciens.";
J. Bacteriol. 188:3329-3336(2006).
[3]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 8-471 IN COMPLEX WITH SODIUM
ION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=18927357; DOI=10.1126/science.1164440;
Weyand S., Shimamura T., Yajima S., Suzuki S., Mirza O., Krusong K.,
Carpenter E.P., Rutherford N.G., Hadden J.M., O'Reilly J., Ma P.,
Saidijam M., Patching S.G., Hope R.J., Norbertczak H.T., Roach P.C.,
Iwata S., Henderson P.J., Cameron A.D.;
"Structure and molecular mechanism of a nucleobase-cation-symport-1
family transporter.";
Science 322:709-713(2008).
[4]
X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 6-471, AND SUBCELLULAR
LOCATION.
PubMed=20413494; DOI=10.1126/science.1186303;
Shimamura T., Weyand S., Beckstein O., Rutherford N.G., Hadden J.M.,
Sharples D., Sansom M.S., Iwata S., Henderson P.J., Cameron A.D.;
"Molecular basis of alternating access membrane transport by the
sodium-hydantoin transporter Mhp1.";
Science 328:470-473(2010).
[5]
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 11-466 IN COMPLEX WITH
SUBSTRATE ANALOGS AND SODIUM ION, FUNCTION, ENZYME REGULATION, AND
MUTAGENESIS OF GLN-42; TRP-117; GLN-121; GLY-219; TRP-220 AND ASN-318.
PubMed=24952894; DOI=10.15252/EMBJ.201387557;
Simmons K.J., Jackson S.M., Brueckner F., Patching S.G., Beckstein O.,
Ivanova E., Geng T., Weyand S., Drew D., Lanigan J., Sharples D.J.,
Sansom M.S., Iwata S., Fishwick C.W., Johnson A.P., Cameron A.D.,
Henderson P.J.;
"Molecular mechanism of ligand recognition by membrane transport
protein, Mhp1.";
EMBO J. 33:1831-1844(2014).
-!- FUNCTION: Nucleobase-proton symporter that mediates the sodium-
dependent binding and uptake of 5-aryl-substituted hydantoin
compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl
hydantoin and 5-benzyl hydantoin are the preferred substrates,
with selectivity for a hydrophobic substituent in position 5 of
hydantoin and for the L isomer over the D isomer (PubMed:16621827,
PubMed:24952894). {ECO:0000269|PubMed:16621827,
ECO:0000269|PubMed:24952894, ECO:0000305|PubMed:16116274}.
-!- ENZYME REGULATION: Inhibited by dinitrophenol, 5-(2-
naphthylmethyl)-D-hydantoin (D-NMH), 5-(2-naphthylmethyl)-L-
hydantoin (L-NMH), 5-bromovinylhydantoin (BVH) and 5-
indolylmethyl-L-hydantoin (L-IMH) (PubMed:16621827,
PubMed:24952894). The affinity of benzyl-hydantoin is increased
over 10-fold in the presence of 15 mM of sodium (PubMed:18927357).
{ECO:0000269|PubMed:16621827, ECO:0000269|PubMed:18927357,
ECO:0000269|PubMed:24952894}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.6. {ECO:0000269|PubMed:16621827};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16621827};
Multi-pass membrane protein {ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:20413494}.
-!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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PDB; 2JLN; X-ray; 2.85 A; A=8-471.
PDB; 2X79; X-ray; 3.80 A; A=6-470.
PDB; 4D1A; X-ray; 3.40 A; A=11-466.
PDB; 4D1B; X-ray; 3.80 A; A=11-466.
PDB; 4D1C; X-ray; 3.70 A; A=11-466.
PDB; 4D1D; X-ray; 3.70 A; A=11-466.
PDBsum; 2JLN; -.
PDBsum; 2X79; -.
PDBsum; 4D1A; -.
PDBsum; 4D1B; -.
PDBsum; 4D1C; -.
PDBsum; 4D1D; -.
SMR; D6R8X8; -.
TCDB; 2.A.39.3.6; the nucleobase:cation symporter-1 (ncs1) family.
EvolutionaryTrace; D6R8X8; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
InterPro; IPR001248; Pur-cyt_permease.
Pfam; PF02133; Transp_cyt_pur; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Membrane; Metal-binding;
Sodium; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 489 Hydantoin permease.
/FTId=PRO_0000439923.
TRANSMEM 30 50 Helical; Name=1. {ECO:0000255}.
TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}.
TRANSMEM 104 124 Helical; Name=3. {ECO:0000255}.
TRANSMEM 144 164 Helical; Name=4. {ECO:0000255}.
TRANSMEM 167 187 Helical; Name=5. {ECO:0000255}.
TRANSMEM 207 227 Helical; Name=6. {ECO:0000255}.
TRANSMEM 258 278 Helical; Name=7. {ECO:0000255}.
TRANSMEM 299 321 Helical; Name=8. {ECO:0000255}.
TRANSMEM 339 359 Helical; Name=9. {ECO:0000255}.
TRANSMEM 362 382 Helical; Name=10. {ECO:0000255}.
TRANSMEM 405 424 Helical; Name=11. {ECO:0000255}.
TRANSMEM 428 445 Helical; Name=12. {ECO:0000255}.
METAL 38 38 Sodium; via carbonyl oxygen.
{ECO:0000244|PDB:2JLN,
ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:24952894}.
METAL 41 41 Sodium; via carbonyl oxygen.
{ECO:0000244|PDB:2JLN,
ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:24952894}.
METAL 309 309 Sodium; via carbonyl oxygen.
{ECO:0000244|PDB:2JLN,
ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:24952894}.
METAL 312 312 Sodium. {ECO:0000244|PDB:2JLN,
ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:24952894}.
METAL 313 313 Sodium. {ECO:0000244|PDB:2JLN,
ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000305|PubMed:18927357,
ECO:0000305|PubMed:24952894}.
BINDING 121 121 Substrate. {ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000269|PubMed:24952894}.
BINDING 219 219 Substrate; via carbonyl oxygen.
{ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000269|PubMed:24952894}.
BINDING 318 318 Substrate. {ECO:0000244|PDB:4D1A,
ECO:0000244|PDB:4D1B,
ECO:0000244|PDB:4D1C,
ECO:0000244|PDB:4D1D,
ECO:0000269|PubMed:24952894}.
MUTAGEN 42 42 Q->F: Strong decrease in uptake and
binding efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 42 42 Q->N: Modest decrease in uptake and
binding efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 117 117 W->A: Reduces dramatically the uptake
efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 117 117 W->F: Reduces moderately the uptake
efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 121 121 Q->N: Partial decrease in efficiency of
both binding and uptake.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 219 219 G->I,S: Reduces both binding and uptake
efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 220 220 W->A,F: Little effect on uptake
efficiency.
{ECO:0000269|PubMed:24952894}.
MUTAGEN 318 318 N->A: Significant loss of uptake activity
and a substantial reduction in binding
efficiency.
{ECO:0000269|PubMed:24952894}.
STRAND 15 18 {ECO:0000244|PDB:4D1A}.
HELIX 22 24 {ECO:0000244|PDB:2JLN}.
HELIX 29 40 {ECO:0000244|PDB:2JLN}.
HELIX 44 52 {ECO:0000244|PDB:2JLN}.
TURN 53 55 {ECO:0000244|PDB:2JLN}.
HELIX 58 79 {ECO:0000244|PDB:2JLN}.
HELIX 81 86 {ECO:0000244|PDB:2JLN}.
HELIX 90 93 {ECO:0000244|PDB:2JLN}.
TURN 94 97 {ECO:0000244|PDB:2JLN}.
TURN 100 103 {ECO:0000244|PDB:2JLN}.
HELIX 104 137 {ECO:0000244|PDB:2JLN}.
HELIX 142 157 {ECO:0000244|PDB:2JLN}.
HELIX 160 190 {ECO:0000244|PDB:2JLN}.
HELIX 194 197 {ECO:0000244|PDB:2JLN}.
HELIX 209 217 {ECO:0000244|PDB:2JLN}.
TURN 218 220 {ECO:0000244|PDB:2JLN}.
HELIX 221 224 {ECO:0000244|PDB:2JLN}.
HELIX 225 227 {ECO:0000244|PDB:2JLN}.
HELIX 228 231 {ECO:0000244|PDB:2JLN}.
HELIX 242 278 {ECO:0000244|PDB:2JLN}.
HELIX 283 291 {ECO:0000244|PDB:2JLN}.
HELIX 296 311 {ECO:0000244|PDB:2JLN}.
HELIX 314 318 {ECO:0000244|PDB:2JLN}.
HELIX 320 329 {ECO:0000244|PDB:2JLN}.
TURN 331 333 {ECO:0000244|PDB:2JLN}.
HELIX 336 349 {ECO:0000244|PDB:2JLN}.
HELIX 352 354 {ECO:0000244|PDB:2JLN}.
HELIX 356 368 {ECO:0000244|PDB:2JLN}.
HELIX 371 382 {ECO:0000244|PDB:2JLN}.
HELIX 391 394 {ECO:0000244|PDB:2JLN}.
STRAND 396 399 {ECO:0000244|PDB:2JLN}.
HELIX 409 423 {ECO:0000244|PDB:2JLN}.
HELIX 426 428 {ECO:0000244|PDB:2JLN}.
HELIX 429 448 {ECO:0000244|PDB:2JLN}.
TURN 449 451 {ECO:0000244|PDB:2JLN}.
HELIX 457 461 {ECO:0000244|PDB:2JLN}.
HELIX 462 466 {ECO:0000244|PDB:2JLN}.
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


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