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ARO1_CLAL4
ID   ARO1_CLAL4              Reviewed;        1568 AA.
AC   C4Y9D5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE     AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN   Name=ARO1 {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=CLUG_04813;
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC       reactions in prechorismate polyaromatic amino acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC       cyclases superfamily. Dehydroquinate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
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DR   EMBL; CH408080; EEQ40685.1; -; Genomic_DNA.
DR   RefSeq; XP_002615931.1; XM_002615885.1.
DR   AlphaFoldDB; C4Y9D5; -.
DR   SMR; C4Y9D5; -.
DR   STRING; 306902.C4Y9D5; -.
DR   PRIDE; C4Y9D5; -.
DR   EnsemblFungi; EEQ40685; EEQ40685; CLUG_04813.
DR   GeneID; 8496038; -.
DR   KEGG; clu:CLUG_04813; -.
DR   VEuPathDB; FungiDB:CLUG_04813; -.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   InParanoid; C4Y9D5; -.
DR   OMA; YCYDDHR; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00086.
DR   UniPathway; UPA00053; UER00087.
DR   UniPathway; UPA00053; UER00088.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   CDD; cd00464; SK; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01356; aroA; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..1568
FT                   /note="Pentafunctional AROM polypeptide"
FT                   /id="PRO_0000406713"
FT   REGION          1..380
FT                   /note="3-dehydroquinate synthase"
FT   REGION          393..842
FT                   /note="EPSP synthase"
FT   REGION          867..1056
FT                   /note="Shikimate kinase"
FT   REGION          1057..1267
FT                   /note="3-dehydroquinase"
FT   REGION          1280..1568
FT                   /note="Shikimate dehydrogenase"
FT   ACT_SITE        254
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        269
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        824
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         43..45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         81..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         112..114
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         128
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         137..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         144
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         150
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         159
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         160
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         177..180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         192..195
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         244
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         258..262
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         265
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         281
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         352
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         874..881
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1568 AA;  171942 MW;  F8E975F2427442AD CRC64;
     MSQVEKVSIL GSDSIHVGYG IQDHIVEETL TNLKSSTYVI ITDSNMEATA PYQTLSSKFE
     AGLKEFRPES RLFYYAVSPG ENNKSRETKA QVEDFLLQKG CTRDTVIIAV GGGVVGDMIG
     FVAATFMRGV RVVQVPTTLL AMVDSSIGGK TAVDTPLGKN FVGAFHQPKY VFVDVSFLTT
     LPTRQFINGM AEVVKTAAIW NEEEFTRLEN FAKTFIAVVT SDNIDLATIK DDLVKTVLES
     IRVKADVVSA DEKESSLRNL LNFGHTIGHA IEAIVTPQAL HGECVAVGMV KEAELARYWG
     VLSPVAVARL VNCIAAYNLP TSVGDKIFVQ RIGHKRHFIQ INTLLEKMAI DKKNDGSKIR
     TVILEAIGKC YQLKAHEVSK QDLSFVLTDE TLVHPFQEET TPKENVVIPP GSKSISNRAL
     ILAALGKGTV RIKNLLHSDD TKHMLAAVAA LKGAEISTED NGDTIVVKGN GGNFITCDEQ
     LYLGNAGTAS RFLTTVASLV NVNEQSNDYT VLTGNARMQE RPVGPLVNAL RANGSEIEYL
     NNEGSLPLKI KAGKGLKGGR VELAATISSQ YVSSILMCAP YAEKEVTLAL VGGKPISQLY
     IDMTIAMMKD FGISVTRDPH EEHTYHIPKG VYSNPGVYEV ESDASSATYP LAFAAMTGTS
     CTVPNIGSSS LQGDARFAVD VLKPMGCTVE QTSTSTTVRG PSKGSLKPLT HVDMEPMTDA
     FLTASVVAAI ANSSVPTQIT GIANQRVKEC NRILAMVDEL AKFGVRAEEL PDGIEIYGID
     YKNLKVPSLE NRGVCTYDDH RVAMSFSLLA GMCPEPVLIT ERSCTGKTWP GWWDVLHTKF
     GVELEGYEEP KDLNDPALLV NKEVNGDKSI VVIGMRAAGK STLSRWIADF MGFELIDLDT
     VFEQTHGDIR EYIKANGWGR FRELEAGIMK EYLTKCSSRH VISTGGGIVE SEESRDILKS
     YTKTGGIVLH LHRDLDETIV FLSSDTTRPA YVSEIKDVWA RREKWYHECS NYHFYSSHCG
     TEEEFKKLRH SFVSYLKTIT GAGLSPVPKG RSFVLSLACS DLNDIAENLE DIVAGCEAIE
     LRVDLLKDYS PSFVADQTAV LRKFVNLPII YTIRTKGQGG NFPDEDVQAL EQLSYLGIKL
     GVDYLDVQLS NSEKFVKSII EKKAFTKIIA THIDLAGLPW TRAEWDNKYN QGISLNADVI
     QLVGFAHAFQ DNIDLEQFRA NHTITPLIAF NAGEHGKLSR VLNRTLTPVT SELLSNVSGN
     GQLTVGEINR CFSEIGGLSR RNFYIVGNPI SHSRSPQLHT AGYEKLNLPH RFSKFETDYA
     QKVYEEVMTK PGFGGLAVTI PLKLDIMKYV SELSESAKII GAVNTVTPLD GQPGKFYGDN
     TDWYGITQSF VRHGVPSFGN SSVNGMVVGG GGTSRAAAFA LHQMGCKKIY MVNRTTSKLH
     EIKSSLPSDF NIEVLETVDQ VEAADPVSLV VSCVPADKPL DSELLNKVER ILYHGKNQEK
     RSFVPTLLDA AYKPRVTPIM KIAEEKFGWA VVPGVEMLVN QGVLQFKVHT VFTPPYKNVY
     EAVVDDNV
 
 
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