ID D0YXD1_PHODD Unreviewed; 442 AA.
AC D0YXD1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN ORFNames=VDA_001671 {ECO:0000313|EMBL:EEZ40644.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40644.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ40644.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40644.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the transport of C4-dicarboxylates.
CC {ECO:0000256|PIRNR:PIRNR004539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + succinate(out) = (S)-malate(out) +
CC succinate(in); Xref=Rhea:RHEA:29327, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00034284};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29329;
CC Evidence={ECO:0000256|ARBA:ARBA00034284};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate(in) + succinate(out) = L-aspartate(out) +
CC succinate(in); Xref=Rhea:RHEA:29343, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000256|ARBA:ARBA00034237};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29345;
CC Evidence={ECO:0000256|ARBA:ARBA00034237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fumarate(in) + succinate(out) = fumarate(out) + succinate(in);
CC Xref=Rhea:RHEA:29323, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000256|ARBA:ARBA00034287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29325;
CC Evidence={ECO:0000256|ARBA:ARBA00034287};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR004539}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|PIRNR:PIRNR004539}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) family.
CC {ECO:0000256|ARBA:ARBA00006413, ECO:0000256|PIRNR:PIRNR004539}.
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DR EMBL; ADBS01000001; EEZ40644.1; -; Genomic_DNA.
DR RefSeq; WP_005298489.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0YXD1; -.
DR GeneID; 57342247; -.
DR eggNOG; COG2704; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015556; F:C4-dicarboxylate transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR004668; Anaer_Dcu_memb_transpt.
DR NCBIfam; TIGR00770; Dcu; 1.
DR PANTHER; PTHR36106; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUB; 1.
DR PANTHER; PTHR36106:SF3; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUB; 1.
DR Pfam; PF03605; DcuA_DcuB; 1.
DR PIRSF; PIRSF004539; C4-dicrbxl_trns; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR004539};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR004539};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR004539};
KW Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR004539}.
FT TRANSMEM 6..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 442 AA; 47651 MW; EA1F9FC3FBC50FE2 CRC64;
MLYLEFLFLL LVLYAGSRFG GIGLGVVSGL GLIVEVFIFR MPPTSPPITV MLIILAVVTC
ASILEAAGGL KYMLQVAERI LRSNPKRVTI LGPLVTYTMT FMLGTGHAVY SIMPIIGDVA
LKNGIRPERP MAASSVASQL AITASPISAA VVYYLAQLSG LNESIHLLTI LMVTVPSTLL
GTILLSLYSL RRGKELADDP EYQARLKDPI WAETIKNTTS TSLNEALPKS AMHAVMLFIL
ALISIVIIAM VPEIRTIGDA KPISMSLVIQ MMMLAFGGLI LLVTRTNVQK VPEGVVFKSG
MVAAIAIFGI AWMSDTYFQY AMPSFKSGIT EMVQNYPWTF ALALFIVSVV VNSQAATARM
MLPVGLAMGL NPALLIGLMP ATYGYFFIPN YPSDIATVNF DVTGTTKIGK WYFNHSFMAP
GLIGVVGACV IGYLLAQVVV PM
//
