S2538_ASPOR
ID S2538_ASPOR Reviewed; 327 AA.
AC Q2UU67;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=AO090009000436;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007150; BAE54898.1; -; Genomic_DNA.
DR RefSeq; XP_001816900.1; XM_001816848.2.
DR AlphaFoldDB; Q2UU67; -.
DR SMR; Q2UU67; -.
DR STRING; 510516.Q2UU67; -.
DR EnsemblFungi; BAE54898; BAE54898; AO090009000436.
DR GeneID; 5988830; -.
DR KEGG; aor:AO090009000436; -.
DR VEuPathDB; FungiDB:AO090009000436; -.
DR HOGENOM; CLU_015166_0_3_1; -.
DR OMA; IRDAPYA; -.
DR Proteomes; UP000006564; Chromosome 1.
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:0015187; F:glycine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:1904983; P:glycine import into mitochondrion; IEA:UniProtKB-UniRule.
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..327
FT /note="Mitochondrial glycine transporter"
FT /id="PRO_0000378928"
FT TRANSMEM 27..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 79..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 139..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 192..215
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 21..104
FT /note="Solcar 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 136..217
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 327 AA; 34455 MW; 6A2497B0E013A362 CRC64;
MSNSAVYAVP QVKKTSATTT SKTTFHFAAG LCSGLSSAIL LQPADLLKTR VQQSQNAALL
PTIKSIISSP NGIRGLWRGT LPSALRTGFG SALYFTSLNA LRQGLAHTGV PVALSSASAN
GKGVASSSAL PKLSNSANLA TGAAARVAAG FVMMPVTVLK VRYESSYYAY GSLYSAGRDI
LRTEGVRGLF AGFGATAARD APYAGLYVLF YEQLKRRFAS LADSGTGDQS LKSSSSSINF
VSGALAAGLA TAITNPFDAV KTRLQLMPNK YGNMMRAVKL MVHEDGVRSL LGGLGLRITR
KALSSALAWT VYEELILRAE KHWATRD
