S2538_SCLS1
ID S2538_SCLS1 Reviewed; 330 AA.
AC A7F9Y3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mitochondrial glycine transporter {ECO:0000255|HAMAP-Rule:MF_03064};
DE AltName: Full=Solute carrier family 25 member 38 homolog {ECO:0000255|HAMAP-Rule:MF_03064};
GN ORFNames=SS1G_14414;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Mitochondrial glycine transporter that imports glycine into
CC the mitochondrial matrix. Plays an important role in providing glycine
CC for the first enzymatic step in heme biosynthesis, the condensation of
CC glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the
CC mitochondrial matrix. {ECO:0000255|HAMAP-Rule:MF_03064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) = glycine(out); Xref=Rhea:RHEA:70715,
CC ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:Q96DW6};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03064}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03064}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC SLC25A38 subfamily. {ECO:0000255|HAMAP-Rule:MF_03064}.
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DR EMBL; CH476653; EDO00544.1; -; Genomic_DNA.
DR RefSeq; XP_001584645.1; XM_001584595.1.
DR AlphaFoldDB; A7F9Y3; -.
DR SMR; A7F9Y3; -.
DR STRING; 665079.A7F9Y3; -.
DR EnsemblFungi; EDO00544; EDO00544; SS1G_14414.
DR GeneID; 5480721; -.
DR KEGG; ssl:SS1G_14414; -.
DR VEuPathDB; FungiDB:sscle_13g096740; -.
DR eggNOG; KOG0766; Eukaryota.
DR HOGENOM; CLU_015166_0_3_1; -.
DR InParanoid; A7F9Y3; -.
DR OMA; IRDAPYA; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904983; P:glycine import into mitochondrion; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:EnsemblFungi.
DR Gene3D; 1.50.40.10; -; 2.
DR HAMAP; MF_03064; SLC25A38; 1.
DR InterPro; IPR030847; Hem25/SLC25A38.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..330
FT /note="Mitochondrial glycine transporter"
FT /id="PRO_0000378944"
FT TRANSMEM 17..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 69..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 128..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 181..204
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 238..264
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 293..311
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 11..94
FT /note="Solcar 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 122..206
FT /note="Solcar 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 234..318
FT /note="Solcar 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
SQ SEQUENCE 330 AA; 35626 MW; F04624E8F632A0AE CRC64;
MSNGGNAGKK SSSYFHFTAG LGSGILSAVL LQPADLLKTR LQQSNHASLL TTIRELSQSP
NTIRSFWRGT VPSALRTGFG SAIYFTSLNA LRQNVARSNL LRTIGVVDAK NGPVHSSSLP
KLSNLANLTT GAVARAGAGF VLMPMTIIKV RYESNLYAYK SIMGAGRDIF LTEGFRGFFS
GFGATAIRDA PYAGLYVLFY EQLKKRLSHI VHSVPQAEEL VENLGVRKNM KGSTSASINF
GSGVLAAGLA TAITNPFDAI KTRIQLQPKK YTNLVMAGRK MVGEEGVKSL FDGLGLRMGR
KAVSSALAWT IYEELIRRAE LAWKGEEVIV
