ID A0A2H0ZPD2_CANAR Unreviewed; 318 AA.
AC A0A2H0ZPD2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=B9J08_001964 {ECO:0000313|EMBL:PIS54820.1}, CA7LBN_003248
GN {ECO:0000313|EMBL:QWW24414.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS54820.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS54820.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS54820.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0000313|EMBL:PIS54820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS54820.1};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida auris genome assembly and annotation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QWW24414.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA7LBN {ECO:0000313|EMBL:QWW24414.1};
RA Finianos M.;
RT "Candida auris outbreak in lebanese hospital.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
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; PEKT02000005; PIS54820.1; -; Genomic_DNA.
DR EMBL; CP076751; QWW24414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H0ZPD2; -.
DR SMR; A0A2H0ZPD2; -.
DR STRING; 498019.A0A2H0ZPD2; -.
DR EnsemblFungi; B9J08_001964-t37_1; B9J08_001964-t37_1-p1; B9J08_001964.
DR VEuPathDB; FungiDB:B9J08_001964; -.
DR VEuPathDB; FungiDB:CJI96_0002637; -.
DR VEuPathDB; FungiDB:CJI97_002149; -.
DR VEuPathDB; FungiDB:CJJ07_004630; -.
DR VEuPathDB; FungiDB:CJJ09_003052; -.
DR VEuPathDB; FungiDB:QG37_08140; -.
DR OMA; WGIYEEL; -.
DR OrthoDB; 5174168at2759; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR Proteomes; UP000825438; Chromosome III.
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 {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:UP000230249};
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 19..104
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 123..212
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 230..317
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 318 AA; 34645 MW; F06A894ACEDA406D CRC64;
MDHEQIPPAP AAPPEVKVPS TKIHLISGGS AGLVSAFTLQ PLDLLKTRLQ QQRRTNTGLK
TSITKELKKL ANIRDLWRGV LPSTLRTSVG AGLYFTILSQ TRTYIASLKK VSEKSSSSVL
PKLSHAENLA TGFVVRAAVG VITMPITIIK TRFESNLYNY NSMYEGFEGI YNEGGGPKGS
FKNFFKGTAA TLARDCPYAG LYVLFYESFK NDVIPSLLVP FRRSIHDNYL ASVTNSSSAV
LAASVATTIT APFDAIKTRL QLIVSVGRPP TIWTATKQII SEPGGVKNLF NGLSLRLGRK
GLSAGISWCI YEELLKFL
//
