ID Q087M5_SHEFN Unreviewed; 415 AA.
AC Q087M5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=C4-dicarboxylate transporter {ECO:0000256|PIRNR:PIRNR004539};
GN OrderedLocusNames=Sfri_0681 {ECO:0000313|EMBL:ABI70540.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70540.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI70540.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70540.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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) + 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; CP000447; ABI70540.1; -; Genomic_DNA.
DR AlphaFoldDB; Q087M5; -.
DR STRING; 318167.Sfri_0681; -.
DR KEGG; sfr:Sfri_0681; -.
DR eggNOG; COG2704; Bacteria.
DR HOGENOM; CLU_036056_1_1_6; -.
DR Proteomes; UP000000684; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000684};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 415 AA; 43047 MW; D4F65F2B053695AA CRC64;
MGSMGIGFAG GVGVLILTAG LGLTPGTIPI DVILIIMSVI TAIAAMQVSG GMDYLVSLAE
KLLRKHPKQI TFLAPVVTYF MTLFAGTGHT AFSTLPVIAE VAKEQGIRPS RPLSIAVVAS
QVAITASPIS AAVVFFSGIL EPLGVDYLVL LAVCIPSTFL ACMVGAVVAN LMGKPLAEDP
IYQDRLAKGL IKKRGATQIN IKDGAKRSVV IFLMAIAAVM IYATAISDKV GLIVNPVLPR
DSAIMVIMLT AAAAITIFCK LDASEISNAA TFKSGMSACV CVLGVAWLGD TFVANHIDEI
KDLAGTLLQS QPWLLSVTLF FASMLLYSQG ATTKALMPAA LAIGVSPLTA VASFAAVSAL
FVLPTYPTLL AAVEMDDTGS TRIGKAVFNH PFLIPGVVTI ATSVALAFLF GGMII
//
