ID S2538_KLULA Reviewed; 294 AA.
AC Q6CNY8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 107.
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 OrderedLocusNames=KLLA0E08911g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382125; CAG99438.1; -; Genomic_DNA.
DR RefSeq; XP_454351.1; XM_454351.1.
DR AlphaFoldDB; Q6CNY8; -.
DR SMR; Q6CNY8; -.
DR STRING; 284590.Q6CNY8; -.
DR PaxDb; 284590-Q6CNY8; -.
DR GeneID; 2894220; -.
DR KEGG; kla:KLLA0_E08911g; -.
DR eggNOG; KOG0766; Eukaryota.
DR HOGENOM; CLU_015166_0_3_1; -.
DR InParanoid; Q6CNY8; -.
DR OMA; WGIYEEL; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:1904983; P:glycine import into mitochondrion; IEA:UniProtKB-UniRule.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR HAMAP; MF_03064; SLC25A38; 1.
DR InterPro; IPR030847; Hem25/SLC25A38.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR46181; MITOCHONDRIAL GLYCINE TRANSPORTER; 1.
DR PANTHER; PTHR46181:SF3; MITOCHONDRIAL GLYCINE TRANSPORTER; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; Mitochondrial carrier; 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..294
FT /note="Mitochondrial glycine transporter"
FT /id="PRO_0000378936"
FT TRANSMEM 11..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 59..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 108..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 161..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 212..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 267..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 5..84
FT /note="Solcar 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 102..186
FT /note="Solcar 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 208..292
FT /note="Solcar 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
SQ SEQUENCE 294 AA; 32692 MW; B2BFF0ECAD4FF2B5 CRC64;
MSEQRRATTH LIGGFSGGLV SAIILQPFDL LKTRLQQDKT STLWKTLKSI ETPSQLWRGA
LPSCIRTSVG SAMYLTMLNS IRQAISKGKN TGSTGSSYLP QLNMYENMFS GAVTRALTGL
ITMPITVIKV RYESTLYQYT SLRYATSHIF RTEGLRGFFR GFGATALRDA PYAGLYMLFY
DRMKVLVPTL LPSNVVKLNS DNRYSTYAST LINGSSAFSA AVIATSITAP FDTVKTRMQL
EPAKFHSFTS TFWHIATKES VRNLFAGISL RLTRKAFSAG IAWGIYEEIV KKFV
//
