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GENK_CORGL
ID   GENK_CORGL              Reviewed;         444 AA.
AC   Q8NLB7; Q6M1I5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Gentisate transporter;
GN   Name=genK; OrderedLocusNames=Cgl3025, cg3353;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF ASP-54; ASP-57; ARG-103; TRP-309; ASP-312; ARG-313; ILE-317
RP   AND ARG-386.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=22808015; DOI=10.1371/journal.pone.0038701;
RA   Xu Y., Wang S.H., Chao H.J., Liu S.J., Zhou N.Y.;
RT   "Biochemical and molecular characterization of the gentisate transporter
RT   GenK in Corynebacterium glutamicum.";
RL   PLoS ONE 7:E38701-E38701(2012).
CC   -!- FUNCTION: Transport of gentisate (2,5-dihydroxybenzoate) into the cell.
CC       Does not transport 3-hydroxybenzoate or benzoate.
CC       {ECO:0000269|PubMed:22808015}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.71 uM for gentisate {ECO:0000269|PubMed:22808015};
CC         Vmax=3.06 nmol/min/mg enzyme {ECO:0000269|PubMed:22808015};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant retains 85% of its transport
CC       activity at pH 6.5, but it loses 79% and 88% activity at pH 7.5 and
CC       8.0, respectively. {ECO:0000269|PubMed:22808015}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Aromatic
CC       acid:H(+) symporter (AAHS) (TC 2.A.1.15) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC00419.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAF18965.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAC00419.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX927157; CAF18965.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_602219.1; NC_003450.3.
DR   RefSeq; WP_011015577.1; NC_003450.3.
DR   AlphaFoldDB; Q8NLB7; -.
DR   SMR; Q8NLB7; -.
DR   STRING; 196627.cg3353; -.
DR   TCDB; 2.A.1.15.10; the major facilitator superfamily (mfs).
DR   KEGG; cgb:cg3353; -.
DR   KEGG; cgl:Cgl3025; -.
DR   PATRIC; fig|196627.13.peg.2960; -.
DR   eggNOG; COG2814; Bacteria.
DR   HOGENOM; CLU_001265_46_4_11; -.
DR   BioCyc; MetaCyc:G18NG-12646-MON; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..444
FT                   /note="Gentisate transporter"
FT                   /id="PRO_0000428627"
FT   TRANSMEM        42..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         54
FT                   /note="D->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         54
FT                   /note="D->E: Retains 50% of its transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         57
FT                   /note="D->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         57
FT                   /note="D->E: Retains 50% of its transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         103
FT                   /note="R->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         309
FT                   /note="W->V: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         312
FT                   /note="D->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         313
FT                   /note="R->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         317
FT                   /note="I->H,Y: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
FT   MUTAGEN         386
FT                   /note="R->A: Loss of transport activity."
FT                   /evidence="ECO:0000269|PubMed:22808015"
SQ   SEQUENCE   444 AA;  46806 MW;  ABFD4C5D5F73608E CRC64;
     MTSHAPESGG LVTESTLGAS NSSQTIENKG LTILGISGRR LAAVLIGWFF VIFDGYDLIV
     YGTVQSALAK EWNLSSATLG TIGSTAFFGM AIGAVFIGRL SDRVGRKAAV IGSVLILSVF
     TMLCAFAPNP WVFGAFRFIA GLGLGGLVPS VNAMTSDLVP RKTMSAWATV MMSGVPIGGS
     IAAVLALVVV PSSEEWGWRF MFLIALIPLV VGLPIAMKVI PSDKAIKADH DIREGHDEPA
     GFKDLLVDRY RWISIWFALA TFVTLLAWYG LGTWLPRLME TAGYEFGHAL MFTLALNLGA
     VIGSVVTAWA GDRFGPIRSG VIAAGIAGIA LLLLLTYPPV TAVYVILILA GVGTHGTQIL
     IIAAVANFYP SNLRGTALGW ALGVGRIGAV VAPQLAGLLL AWNLGVNSNF IMFGTAALLS
     ALALSVLLRL QKTYSVTHKV EIQG
 
 
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