FBT_SYNY3
ID FBT_SYNY3 Reviewed; 494 AA.
AC Q55721;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Folate-biopterin transporter;
GN OrderedLocusNames=slr0642;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION.
RX PubMed=16162503; DOI=10.1074/jbc.m507432200;
RA Klaus S.M., Kunji E.R., Bozzo G.G., Noiriel A., de la Garza R.D.,
RA Basset G.J., Ravanel S., Rebeille F., Gregory J.F. III, Hanson A.D.;
RT "Higher plant plastids and cyanobacteria have folate carriers related to
RT those of trypanosomatids.";
RL J. Biol. Chem. 280:38457-38463(2005).
RN [3]
RP MUTAGENESIS OF ARG-53; LYS-61; ASP-62; TRP-82; LYS-85; ASP-93; ASP-145;
RP ASP-149; ARG-155; PHE-252; THR-259; GLU-263; PHE-267; ARG-309; ARG-335;
RP ASP-348; GLN-357; ARG-369; CYS-371; PHE-380; MET-384 AND ASN-388, AND
RP FUNCTION.
RX PubMed=19923217; DOI=10.1074/jbc.m109.063651;
RA Eudes A., Kunji E.R., Noiriel A., Klaus S.M., Vickers T.J., Beverley S.M.,
RA Gregory J.F. III, Hanson A.D.;
RT "Identification of transport-critical residues in a folate transporter from
RT the folate-biopterin transporter (FBT) family.";
RL J. Biol. Chem. 285:2867-2875(2010).
CC -!- FUNCTION: Mediates folate monoglutamate transport involved in
CC tetrahydrofolate biosynthesis. It also mediates transport of
CC antifolates, such as methotrexate and aminopterin.
CC {ECO:0000269|PubMed:16162503, ECO:0000269|PubMed:19923217}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Folate-
CC biopterin transporter (TC 2.A.71) family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10362.1; -; Genomic_DNA.
DR PIR; S76516; S76516.
DR AlphaFoldDB; Q55721; -.
DR IntAct; Q55721; 9.
DR STRING; 1148.1001631; -.
DR TCDB; 2.A.71.2.3; the folate-biopterin transporter (fbt) family.
DR PaxDb; Q55721; -.
DR PRIDE; Q55721; -.
DR EnsemblBacteria; BAA10362; BAA10362; BAA10362.
DR KEGG; syn:slr0642; -.
DR eggNOG; COG2211; Bacteria.
DR InParanoid; Q55721; -.
DR OMA; GIDDHWF; -.
DR PhylomeDB; Q55721; -.
DR Proteomes; UP000001425; Chromosome.
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:0015231; F:5-formyltetrahydrofolate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008517; F:folic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015350; F:methotrexate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015885; P:5-formyltetrahydrofolate transport; IDA:UniProtKB.
DR GO; GO:0015884; P:folic acid transport; IDA:UniProtKB.
DR GO; GO:0051958; P:methotrexate transport; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR039309; BT1.
DR InterPro; IPR004324; FBT.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR31585; PTHR31585; 1.
DR Pfam; PF03092; BT1; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00788; fbt; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..494
FT /note="Folate-biopterin transporter"
FT /id="PRO_0000420112"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 441..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53
FT /note="R->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 61
FT /note="K->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 62
FT /note="D->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 82
FT /note="W->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 85
FT /note="K->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 93
FT /note="D->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 145
FT /note="D->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 149
FT /note="D->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 155
FT /note="R->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 252
FT /note="F->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 259
FT /note="T->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 263
FT /note="E->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 267
FT /note="F->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 309
FT /note="R->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 335
FT /note="R->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 348
FT /note="D->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 357
FT /note="Q->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 369
FT /note="R->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 371
FT /note="C->A: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 380
FT /note="F->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 384
FT /note="M->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
FT MUTAGEN 388
FT /note="N->C: Affects 5-formyltetrahydrofolate transporter
FT activity."
FT /evidence="ECO:0000269|PubMed:19923217"
SQ SEQUENCE 494 AA; 53586 MW; 101BAB039B77E66A CRC64;
MLVAMSMTPI AILFSTPLKR FLREKVLLGN APSWELLAIL SIYFVQGVLG LSRLAVSFFL
KDELGLSPAA MGALIGLGAA PWILKPVLGL MSDTVPLFGY RRRSYLWLSG LMGSAGWLLF
AAWVSSGTQA GLVLLFTSLS VAIGDVIVDS LVVERAQRES LAQVGSLQSL TWGAAAVGGI
ITAYASGALL EWFSTRTVFA ITAIFPLLTV GAAFLISEVS TAEEEEKPQP KAQIKLVWQA
VRQKTILLPT LFIFFWQATP SAESAFFYFT TNELGFEPKF LGRVRLVTSV AGLIGVGLYQ
RFLKTLPFRV IMGWSTVISS LLGLTTLILI THANRAMGID DHWFSLGDSI ILTVTGQIAF
MPVLVLAARL CPPGIEATLF ALLMSVMNLA GVLSFEVGSL LTHWLGVTET QFDNLALLVI
ITNLSTLLPL PFLGLLPAGD PQVKDKTEKE DNPDDPGDRL VLPPAEVFEH HTVGSLSDQN
FLPEFFPEKS SSRP