ID Q7MGV7_VIBVY Unreviewed; 435 AA.
AC Q7MGV7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN OrderedLocusNames=VV3119 {ECO:0000313|EMBL:BAC95883.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC95883.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC95883.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC95883.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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) + L-aspartate(out) = fumarate(out) + L-
CC aspartate(in); Xref=Rhea:RHEA:72459, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:29991; Evidence={ECO:0000256|ARBA:ARBA00036117};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72460;
CC Evidence={ECO:0000256|ARBA:ARBA00036117};
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; BA000037; BAC95883.1; -; Genomic_DNA.
DR RefSeq; WP_011151356.1; NC_005139.1.
DR AlphaFoldDB; Q7MGV7; -.
DR STRING; 672.VV93_v1c28410; -.
DR KEGG; vvy:VV3119; -.
DR PATRIC; fig|196600.6.peg.3093; -.
DR eggNOG; COG2704; Bacteria.
DR HOGENOM; CLU_036056_1_1_6; -.
DR Proteomes; UP000002675; Chromosome I.
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:SF2; ANAEROBIC C4-DICARBOXYLATE TRANSPORTER DCUA; 1.
DR PANTHER; PTHR36106; 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 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..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..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..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 435 AA; 45301 MW; BD70E7594CBA2247 CRC64;
MVAVELLVVL LFIYLGARIG GIGIGFAGGA GVIVLSLILG VPTKQAFIPV DVILIIMSVI
TAIAAMQVAG GMDWLVQIAE NFLRKHPERI TFYAPIVTFL MTLMAGTGHT AFSTLPVIAE
VAKGQGVRPS RPLSIAVVAS QIAITASPIS AAVVAFAAML APFGVDYLTL LAVCIPTTFV
ACMIGALVAN YMGSELKDDP EYQDRLEKGL IKLSTETQRE ILPTAKTATY IFLGAIAFVV
CYAAAISSSV GLIENPALGR NEAIMTVMLA AAAAIVMFTK IDASKIPSAA TFRSGMTACV
CVLGVAWLGS TFVNAHVDGI KDVAGALLSD YPWMLALVLF FASMLLYSQG ATTVALMPAA
LAIGVAPLTA VASFAAVSAL FVLPTYPTLL AAVEMDDTGS TRIGKYVFNH PFFIPGVVTI
ASAVALGFAF GSLFI
//
