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S2538_BOTFB
ID   S2538_BOTFB             Reviewed;         332 AA.
AC   A6S8E0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=BC1G_09631;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
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; CH476897; EDN29458.1; -; Genomic_DNA.
DR   RefSeq; XP_001552401.1; XM_001552351.1.
DR   AlphaFoldDB; A6S8E0; -.
DR   SMR; A6S8E0; -.
DR   GeneID; 5432934; -.
DR   KEGG; bfu:BCIN_11g00520; -.
DR   VEuPathDB; FungiDB:Bcin11g00520; -.
DR   OMA; IRDAPYA; -.
DR   OrthoDB; 1531343at2759; -.
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; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..332
FT                   /note="Mitochondrial glycine transporter"
FT                   /id="PRO_0000378930"
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        127..152
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        180..203
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        239..265
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        294..312
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          121..205
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   REPEAT          235..319
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
SQ   SEQUENCE   332 AA;  35765 MW;  EF74B5F66FDDB601 CRC64;
     MSNGGNAGKK SSSYFHFGAG LGSGILSAVL LQPADLLKTR VQQSNHASLF TTIRELSQSP
     NSIRSFWRGT VPSALRTGFG SAIYFTSLNA LRQNVARSNL LRTIGVVEQK SMVHSSSLPK
     LSNLANLTTG AVARAGAGFI LMPMTIIKVR YESNLYAYKS IAGAGRDIFL TEGFRGFFSG
     FGATAIRDAP YAGLYVLFYE ELKKRLSHIV HSSPQVEGLA EKVDLGLSKN MKGSTSASIN
     FGSGVLAAGL ATAITNPFDA IKTRIQLQPK KYTNLVMAGK KMVGEEGVKS LFDGLGLRMG
     RKAVSSALAW TIYEELIRRA EAVLKREKEL VV
 
 
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