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MEND_ECOLI
ID   MEND_ECOLI              Reviewed;         556 AA.
AC   P17109; P76478; P78180; P78181;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 4.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE            Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE            EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659};
DE   AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659};
GN   Name=menD {ECO:0000255|HAMAP-Rule:MF_01659};
GN   OrderedLocusNames=b2264, JW5374;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8764478; DOI=10.1016/0378-1097(96)00173-5;
RA   Daruwala R., Kwon O., Meganathan R., Hudspeth M.E.S.;
RT   "A new isochorismate synthase specifically involved in menaquinone (vitamin
RT   K2) biosynthesis encoded by the menF gene.";
RL   FEMS Microbiol. Lett. 140:159-163(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-507.
RX   PubMed=2666397; DOI=10.1128/jb.171.8.4349-4354.1989;
RA   Popp J.L.;
RT   "Sequence and overexpression of the menD gene from Escherichia coli.";
RL   J. Bacteriol. 171:4349-4354(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 536-556.
RC   STRAIN=K12;
RA   Sharma V., Hudspeth M.E., Meganathan R.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INDUCTION, AND PRELIMINARY FUNCTION.
RC   STRAIN=K12;
RX   PubMed=1459959; DOI=10.1128/jb.174.24.8111-8118.1992;
RA   Palaniappan C., Sharma V., Hudspeth M.E., Meganathan R.;
RT   "Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia coli
RT   menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic
RT   acid synthase and alpha-ketoglutarate decarboxylase activities.";
RL   J. Bacteriol. 174:8111-8118(1992).
RN   [8]
RP   SUBUNIT, COFACTOR, MUTAGENESIS OF GLU-55, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=14621995; DOI=10.1021/bi035224j;
RA   Bhasin M., Billinsky J.L., Palmer D.R.J.;
RT   "Steady-state kinetics and molecular evolution of Escherichia coli MenD
RT   [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase],
RT   an anomalous thiamin diphosphate-dependent decarboxylase-carboligase.";
RL   Biochemistry 42:13496-13504(2003).
RN   [9]
RP   CRYSTALLIZATION, COFACTOR, AND SUBUNIT.
RX   PubMed=16511076; DOI=10.1107/s1744309105010997;
RA   Sieminska E.A.L., Macova A., Palmer D.R.J., Sanders D.A.R.;
RT   "Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-
RT   hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from
RT   Escherichia coli.";
RL   Acta Crystallogr. F 61:489-492(2005).
RN   [10]
RP   FUNCTION AS A SEPHCHC SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17760421; DOI=10.1021/bi700810x;
RA   Jiang M., Cao Y., Guo Z.-F., Chen M., Chen X., Guo Z.;
RT   "Menaquinone biosynthesis in Escherichia coli: identification of 2-
RT   succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel
RT   intermediate and re-evaluation of MenD activity.";
RL   Biochemistry 46:10979-10989(2007).
CC   -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation
CC       of 2-oxoglutarate and the subsequent addition of the resulting succinic
CC       semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-
CC       succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
CC       {ECO:0000255|HAMAP-Rule:MF_01659, ECO:0000269|PubMed:17760421}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-
CC         hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2;
CC         Xref=Rhea:RHEA:25593, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29780, ChEBI:CHEBI:58818; EC=2.2.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659,
CC         ECO:0000269|PubMed:17760421};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01659};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=53 nM for isochorismate (at 22.5 degrees Celsius and pH 7.8)
CC         {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421};
CC         KM=1.5 uM for 2-oxoglutarate (at 22.5 degrees Celsius and pH 7.8)
CC         {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421};
CC         KM=2.4 uM for thiamine diphosphate (at 22.5 degrees Celsius and pH
CC         7.8) {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421};
CC         KM=80 uM for magnesium ions (at 22.5 degrees Celsius and pH 7.8)
CC         {ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:17760421};
CC       pH dependence:
CC         Optimum pH is 7-8. {ECO:0000269|PubMed:14621995,
CC         ECO:0000269|PubMed:17760421};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
CC       {ECO:0000255|HAMAP-Rule:MF_01659}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01659}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659,
CC       ECO:0000269|PubMed:14621995, ECO:0000269|PubMed:16511076}.
CC   -!- INDUCTION: By isopropyl-beta-D-thiogalactoside (IPTG).
CC       {ECO:0000269|PubMed:1459959}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01659, ECO:0000305}.
CC   -!- CAUTION: Was originally thought (PubMed:1459959, PubMed:14621995 and
CC       PubMed:16511076) to be a 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) synthase but further protein analysis clearly
CC       suggests that it is a 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-
CC       1-carboxylate (SEPHCHC) synthase. {ECO:0000305|PubMed:17760421}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24153.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U54790; AAC44304.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75324.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16089.2; -; Genomic_DNA.
DR   EMBL; M21787; AAA24153.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L04464; AAB59060.1; -; Genomic_DNA.
DR   EMBL; L35030; AAA24150.1; -; Genomic_DNA.
DR   PIR; F64997; F64997.
DR   RefSeq; NP_416767.1; NC_000913.3.
DR   RefSeq; WP_001295284.1; NZ_STEB01000008.1.
DR   PDB; 2JLA; X-ray; 2.81 A; A/B/C/D=1-556.
DR   PDB; 2JLC; X-ray; 2.50 A; A/B=1-556.
DR   PDB; 3FLM; X-ray; 2.70 A; A/B=1-556.
DR   PDB; 3HWW; X-ray; 1.95 A; A/D=1-556.
DR   PDB; 3HWX; X-ray; 2.60 A; 1/A/B/I/J/R/S/Z=1-556.
DR   PDB; 5EJ4; X-ray; 1.77 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJ5; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJ6; X-ray; 2.24 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJ7; X-ray; 1.56 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJ8; X-ray; 1.34 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJ9; X-ray; 1.72 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJA; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5EJM; X-ray; 1.72 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5Z2P; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5Z2R; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-556.
DR   PDB; 5Z2U; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-556.
DR   PDBsum; 2JLA; -.
DR   PDBsum; 2JLC; -.
DR   PDBsum; 3FLM; -.
DR   PDBsum; 3HWW; -.
DR   PDBsum; 3HWX; -.
DR   PDBsum; 5EJ4; -.
DR   PDBsum; 5EJ5; -.
DR   PDBsum; 5EJ6; -.
DR   PDBsum; 5EJ7; -.
DR   PDBsum; 5EJ8; -.
DR   PDBsum; 5EJ9; -.
DR   PDBsum; 5EJA; -.
DR   PDBsum; 5EJM; -.
DR   PDBsum; 5Z2P; -.
DR   PDBsum; 5Z2R; -.
DR   PDBsum; 5Z2U; -.
DR   AlphaFoldDB; P17109; -.
DR   SMR; P17109; -.
DR   BioGRID; 4260506; 9.
DR   BioGRID; 851061; 2.
DR   DIP; DIP-10185N; -.
DR   IntAct; P17109; 1.
DR   STRING; 511145.b2264; -.
DR   jPOST; P17109; -.
DR   PaxDb; P17109; -.
DR   PRIDE; P17109; -.
DR   EnsemblBacteria; AAC75324; AAC75324; b2264.
DR   EnsemblBacteria; BAA16089; BAA16089; BAA16089.
DR   GeneID; 946720; -.
DR   KEGG; ecj:JW5374; -.
DR   KEGG; eco:b2264; -.
DR   PATRIC; fig|511145.12.peg.2357; -.
DR   EchoBASE; EB0574; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_6; -.
DR   InParanoid; P17109; -.
DR   OMA; FCNRGTS; -.
DR   PhylomeDB; P17109; -.
DR   BioCyc; EcoCyc:MEND-MON; -.
DR   BioCyc; MetaCyc:MEND-MON; -.
DR   BRENDA; 2.2.1.9; 2026.
DR   SABIO-RK; P17109; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   EvolutionaryTrace; P17109; -.
DR   PRO; PR:P17109; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc.
DR   DisProt; DP02750; -.
DR   HAMAP; MF_01659; MenD; 1.
DR   InterPro; IPR004433; MenaQ_synth_MenD.
DR   InterPro; IPR032264; MenD_middle.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR42916; PTHR42916; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF16582; TPP_enzyme_M_2; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF004983; MenD; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00173; menD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Magnesium; Manganese; Menaquinone biosynthesis;
KW   Metal-binding; Reference proteome; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..556
FT                   /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT                   carboxylate synthase"
FT                   /id="PRO_0000090829"
FT   MUTAGEN         55
FT                   /note="E->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:14621995"
FT   CONFLICT        42
FT                   /note="Missing (in Ref. 5; AAA24153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..183
FT                   /note="GVHINCPFAEPLYGEMDDTGL -> ESISTARLLNRCMAKWTIPGF (in
FT                   Ref. 5; AAA24153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="Missing (in Ref. 5; AAA24153)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543..556
FT                   /note="AQTLQQLLAQVSHL -> RKRSSNFWRR (in Ref. 6; AAB59060)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..19
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:3FLM"
FT   HELIX           35..43
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           55..69
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           87..96
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   TURN            123..128
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           145..157
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           183..187
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           188..194
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          222..226
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           231..244
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   TURN            252..254
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           263..266
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           270..276
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          280..287
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           292..300
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          304..312
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          322..328
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           330..336
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           349..361
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   TURN            362..365
FT                   /evidence="ECO:0007829|PDB:2JLC"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:5EJ9"
FT   HELIX           369..374
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          385..388
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           392..400
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:2JLC"
FT   STRAND          418..420
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           421..432
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          436..441
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           442..447
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           449..456
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          462..468
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           474..477
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           482..488
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           498..503
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          507..509
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           514..524
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   STRAND          527..536
FT                   /evidence="ECO:0007829|PDB:5EJ8"
FT   HELIX           541..554
FT                   /evidence="ECO:0007829|PDB:5EJ8"
SQ   SEQUENCE   556 AA;  61367 MW;  278201D02243E76D CRC64;
     MSVSAFNRRW AAVILEALTR HGVRHICIAP GSRSTPLTLA AAENSAFIHH THFDERGLGH
     LALGLAKVSK QPVAVIVTSG TAVANLYPAL IEAGLTGEKL ILLTADRPPE LIDCGANQAI
     RQPGMFASHP THSISLPRPT QDIPARWLVS TIDHALGTLH AGGVHINCPF AEPLYGEMDD
     TGLSWQQRLG DWWQDDKPWL REAPRLESEK QRDWFFWRQK RGVVVAGRMS AEEGKKVALW
     AQTLGWPLIG DVLSQTGQPL PCADLWLGNA KATSELQQAQ IVVQLGSSLT GKRLLQWQAS
     CEPEEYWIVD DIEGRLDPAH HRGRRLIANI ADWLELHPAE KRQPWCVEIP RLAEQAMQAV
     IARRDAFGEA QLAHRICDYL PEQGQLFVGN SLVVRLIDAL SQLPAGYPVY SNRGASGIDG
     LLSTAAGVQR ASGKPTLAIV GDLSALYDLN ALALLRQVSA PLVLIVVNNN GGQIFSLLPT
     PQSERERFYL MPQNVHFEHA AAMFELKYHR PQNWQELETA FADAWRTPTT TVIEMVVNDT
     DGAQTLQQLL AQVSHL
 
 
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