ID A0A1E4S3X7_CYBJN Unreviewed; 295 AA.
AC A0A1E4S3X7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Mitochondrial glycine transporter {ECO:0000256|HAMAP-Rule:MF_03064};
DE AltName: Full=Solute carrier family 25 member 38 homolog {ECO:0000256|HAMAP-Rule:MF_03064};
GN ORFNames=CYBJADRAFT_125437 {ECO:0000313|EMBL:ODV74112.1},
GN CYBJADRAFT_132754 {ECO:0000313|EMBL:ODV70862.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV74112.1, ECO:0000313|Proteomes:UP000094389};
RN [1] {ECO:0000313|EMBL:ODV74112.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389}, and NRRL Y-1542
RC {ECO:0000313|EMBL:ODV74112.1};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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 miochondrial matrix. {ECO:0000256|HAMAP-Rule:MF_03064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) = glycine(out); Xref=Rhea:RHEA:70715,
CC ChEBI:CHEBI:57305; Evidence={ECO:0000256|ARBA:ARBA00034060,
CC ECO:0000256|HAMAP-Rule:MF_03064};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|HAMAP-
CC Rule:MF_03064}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|HAMAP-Rule:MF_03064}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC SLC25A38 subfamily. {ECO:0000256|HAMAP-Rule:MF_03064}.
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DR EMBL; KV453949; ODV70862.1; -; Genomic_DNA.
DR EMBL; KV453928; ODV74112.1; -; Genomic_DNA.
DR RefSeq; XP_020067901.1; XM_020213072.1.
DR RefSeq; XP_020071151.1; XM_020212592.1.
DR STRING; 983966.A0A1E4S3X7; -.
DR GeneID; 30986988; -.
DR GeneID; 30987468; -.
DR OrthoDB; 5174168at2759; -.
DR Proteomes; UP000094389; Unassembled WGS sequence.
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; 2.
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 {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03064};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03064};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|HAMAP-Rule:MF_03064};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_03064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03064};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03064};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03064}.
FT REPEAT 3..82
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 104..188
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 206..290
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 295 AA; 32141 MW; 64DC6476FCFD796E CRC64;
MSEKPISHLI GGFAGGLTSA VILQPFDLVK TRLQQQPSGS IPDTLRTLSS YKELWRGTLP
SAVRTSVGSA LYLTSLHAFR SVLAKSHNSS ATNVSGSSSS LPKLSMAENL VTGGLTRGFV
GFVTMPITVL KVRYESTVYQ YDSLLGAVRS IHQTEGVKGF FRGFTATCMR DAPYAGLYVL
FYEQCKMVLP KMLPNVDTGT TLSVSKSAMI NSLSAFSAAS IATTITGPFD TIKTRMQLKP
LEFTGFWQAG VKIVREEGAI RLFDGLSLRL TRKAFSAGIA WGIYEEIIKY IVRQH
//
