ID A0A0N5BZJ2_STREA Unreviewed; 206 AA.
AC A0A0N5BZJ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000256|ARBA:ARBA00040264};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001118200.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001118200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-
CC oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) +
CC maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30780; Evidence={ECO:0000256|ARBA:ARBA00036076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) +
CC malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036366};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) +
CC oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000256|ARBA:ARBA00036462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) +
CC succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00036084};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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DR STRING; 174720.A0A0N5BZJ2; -.
DR WBParaSite; SPAL_0001118200.1; SPAL_0001118200.1; SPAL_0001118200.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45618:SF9; MITOCHONDRIAL 2-OXOGLUTARATE_MALATE CARRIER PROTEIN; 1.
DR PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 2.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 10..94
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 103..192
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 206 AA; 23453 MW; CB4F1292B6704EBF CRC64;
XYHFKQHKQQ QGLSDRVIGS FAGNPTGIAF IRMTGDGRLP PEQRRNYKNV FNSIFRVVRE
ERLFTLWRGC TPTIMRAMVV SVAQLATYSQ AKEMILKSKV VEDGIFCHFL VLMVSGLATT
IISMPVDIVK TRIQSMRVVD GKPEYSGMAD VVKKVISKKG FFALWKCFKP YYLADGEYIA
LTLILLEQLF STYNKYILGH KVANTL
//