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BIRA_ECOLI
ID   BIRA_ECOLI              Reviewed;         321 AA.
AC   P06709; Q2M8R4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 196.
DE   RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000255|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin operon repressor {ECO:0000255|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE            EC=6.3.4.15 {ECO:0000255|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin--protein ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE   AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000255|HAMAP-Rule:MF_00978};
GN   Name=birA {ECO:0000255|HAMAP-Rule:MF_00978}; Synonyms=bioR, dhbB;
GN   OrderedLocusNames=b3973, JW3941;
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=3899863; DOI=10.1016/0378-1119(85)90011-3;
RA   Howard P.K., Shaw J., Otsuka A.J.;
RT   "Nucleotide sequence of the birA gene encoding the biotin operon repressor
RT   and biotin holoenzyme synthetase functions of Escherichia coli.";
RL   Gene 35:321-331(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3536662; DOI=10.1016/0378-1119(86)90189-7;
RA   Buoncristiani M.R., Howard P.K., Otsuka A.J.;
RT   "DNA-binding and enzymatic domains of the bifunctional biotin operon
RT   repressor (BirA) of Escherichia coli.";
RL   Gene 44:255-261(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RC   STRAIN=RDD012;
RX   PubMed=1311302; DOI=10.1128/jb.174.5.1690-1693.1992;
RA   Pucci M.J., Discotto L.F., Dougherty T.J.;
RT   "Cloning and identification of the Escherichia coli murB DNA sequence,
RT   which encodes UDP-N-acetylenolpyruvoylglucosamine reductase.";
RL   J. Bacteriol. 174:1690-1693(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-321.
RX   PubMed=1328157; DOI=10.1128/jb.174.20.6411-6417.1992;
RA   Song W.-J., Jackowski S.;
RT   "Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene
RT   of Escherichia coli.";
RL   J. Bacteriol. 174:6411-6417(1992).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=6129246; DOI=10.1016/s0021-9258(18)33408-2;
RA   Eisenberg M.A., Prakash O., Hsiung S.C.;
RT   "Purification and properties of the biotin repressor. A bifunctional
RT   protein.";
RL   J. Biol. Chem. 257:15167-15173(1982).
RN   [9]
RP   FUNCTION.
RX   PubMed=2667763; DOI=10.1016/0092-8674(89)90421-2;
RA   Cronan J.E. Jr.;
RT   "The E. coli bio operon: transcriptional repression by an essential protein
RT   modification enzyme.";
RL   Cell 58:427-429(1989).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8003500; DOI=10.1021/bi00189a041;
RA   Xu Y., Beckett D.;
RT   "Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia
RT   coli repressor of biotin biosynthesis and the stability of the enzyme-
RT   product complex.";
RL   Biochemistry 33:7354-7360(1994).
RN   [11]
RP   FUNCTION, DNA-BINDING, AND SUBUNIT.
RX   PubMed=12527300; DOI=10.1016/s0022-2836(02)01308-6;
RA   Streaker E.D., Beckett D.;
RT   "Coupling of protein assembly and DNA binding: biotin repressor
RT   dimerization precedes biotin operator binding.";
RL   J. Mol. Biol. 325:937-948(2003).
RN   [12]
RP   DOMAIN, AND MUTAGENESIS OF THR-52; GLY-57 AND TYR-58.
RC   STRAIN=K12;
RX   PubMed=24189073; DOI=10.1074/jbc.m113.525618;
RA   Chakravartty V., Cronan J.E.;
RT   "The wing of a winged helix-turn-helix transcription factor organizes the
RT   active site of BirA, a bifunctional repressor/ligase.";
RL   J. Biol. Chem. 288:36029-36039(2013).
RN   [13]
RP   ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH BCCP.
RX   PubMed=23896299; DOI=10.1016/j.jmb.2013.07.029;
RA   Adikaram P.R., Beckett D.;
RT   "Protein:protein interactions in control of a transcriptional switch.";
RL   J. Mol. Biol. 425:4584-4594(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH BIOTIN, AND DOMAIN.
RX   PubMed=1409631; DOI=10.1073/pnas.89.19.9257;
RA   Wilson K.P., Shewchuk L.M., Brennan R.G., Otsuka A.J., Matthews B.W.;
RT   "Escherichia coli biotin holoenzyme synthetase/bio repressor crystal
RT   structure delineates the biotin- and DNA-binding domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9257-9261(1992).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH BIOTIN, SUBUNIT, AND
RP   DOMAIN.
RX   PubMed=11353844; DOI=10.1073/pnas.111128198;
RA   Weaver L.H., Kwon K., Beckett D., Matthews B.W.;
RT   "Corepressor-induced organization and assembly of the biotin repressor: a
RT   model for allosteric activation of a transcriptional regulator.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6045-6050(2001).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH BIOTINOL-5'-AMP,
RP   SUBUNIT, AND DOMAIN.
RX   PubMed=16438984; DOI=10.1016/j.jmb.2005.12.066;
RA   Wood Z.A., Weaver L.H., Brown P.H., Beckett D., Matthews B.W.;
RT   "Co-repressor induced order and biotin repressor dimerization: a case for
RT   divergent followed by convergent evolution.";
RL   J. Mol. Biol. 357:509-523(2006).
CC   -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a
CC       biotin-operon repressor. In the presence of ATP, BirA activates biotin
CC       to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA)
CC       complex. HoloBirA can either transfer the biotinyl moiety to the biotin
CC       carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or
CC       bind to the biotin operator site and inhibit transcription of the
CC       operon. {ECO:0000255|HAMAP-Rule:MF_00978, ECO:0000269|PubMed:12527300,
CC       ECO:0000269|PubMed:2667763, ECO:0000269|PubMed:6129246,
CC       ECO:0000269|PubMed:8003500}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC         N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC         EC=6.3.4.15; Evidence={ECO:0000255|HAMAP-Rule:MF_00978,
CC         ECO:0000269|PubMed:6129246, ECO:0000269|PubMed:8003500};
CC   -!- ACTIVITY REGULATION: The switch between the enzymatic activity and the
CC       repressor activity is regulated by cellular demand for biotin. The
CC       switch occurs by swapping of protein interaction partners by holoBirA.
CC       In conditions of high biotin demand, holoBirA associates with apoBCCP
CC       to transfer biotin. In conditions of low biotin demand, holoBirA
CC       dimerizes, binds DNA and represses transcription of the biotin operon.
CC       {ECO:0000269|PubMed:23896299}.
CC   -!- SUBUNIT: Monomer in solution. Interacts with BCCP. Homodimerizes to
CC       bind DNA. Interaction with the corepressor bio-5'-AMP increases
CC       dimerization. {ECO:0000269|PubMed:11353844,
CC       ECO:0000269|PubMed:12527300, ECO:0000269|PubMed:1409631,
CC       ECO:0000269|PubMed:16438984, ECO:0000269|PubMed:23896299,
CC       ECO:0000269|PubMed:6129246}.
CC   -!- INTERACTION:
CC       P06709; P0A761: nanE; NbExp=2; IntAct=EBI-545740, EBI-561432;
CC   -!- DOMAIN: Contains an N-terminal helix-turn-helix DNA-binding domain,
CC       connected via a linker to the central catalytic domain and the C-
CC       terminal domain, which plays roles in dimerization, catalytic function
CC       and DNA binding. The N-terminal domain is required for both ligase and
CC       repressor activities. It may orient the active site and thereby play an
CC       important role in enzymatic activity. {ECO:0000269|PubMed:11353844,
CC       ECO:0000269|PubMed:1409631, ECO:0000269|PubMed:16438984,
CC       ECO:0000269|PubMed:24189073}.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00978}.
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DR   EMBL; M10123; AAA23520.1; -; Genomic_DNA.
DR   EMBL; M15820; AAA23521.1; -; Genomic_DNA.
DR   EMBL; L14557; AAA24186.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43075.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76951.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77342.1; -; Genomic_DNA.
DR   PIR; B24029; BVECBF.
DR   RefSeq; NP_418404.1; NC_000913.3.
DR   RefSeq; WP_000654630.1; NZ_SSZK01000084.1.
DR   PDB; 1BIA; X-ray; 2.30 A; A=1-321.
DR   PDB; 1BIB; X-ray; 2.80 A; A=1-321.
DR   PDB; 1HXD; X-ray; 2.40 A; A/B=1-321.
DR   PDB; 2EWN; X-ray; 2.80 A; A/B=1-321.
DR   PDB; 4WF2; X-ray; 2.31 A; A=1-321.
DR   PDBsum; 1BIA; -.
DR   PDBsum; 1BIB; -.
DR   PDBsum; 1HXD; -.
DR   PDBsum; 2EWN; -.
DR   PDBsum; 4WF2; -.
DR   AlphaFoldDB; P06709; -.
DR   SMR; P06709; -.
DR   BioGRID; 4263391; 269.
DR   DIP; DIP-9224N; -.
DR   IntAct; P06709; 7.
DR   STRING; 511145.b3973; -.
DR   BindingDB; P06709; -.
DR   ChEMBL; CHEMBL3559644; -.
DR   DrugBank; DB04651; BIOTINOL-5-AMP.
DR   MoonProt; P06709; -.
DR   jPOST; P06709; -.
DR   PaxDb; P06709; -.
DR   PRIDE; P06709; -.
DR   EnsemblBacteria; AAC76951; AAC76951; b3973.
DR   EnsemblBacteria; BAE77342; BAE77342; BAE77342.
DR   GeneID; 58463579; -.
DR   GeneID; 948469; -.
DR   KEGG; ecj:JW3941; -.
DR   KEGG; eco:b3973; -.
DR   PATRIC; fig|1411691.4.peg.2735; -.
DR   EchoBASE; EB0121; -.
DR   eggNOG; COG0340; Bacteria.
DR   eggNOG; COG1654; Bacteria.
DR   HOGENOM; CLU_051096_4_0_6; -.
DR   InParanoid; P06709; -.
DR   OMA; AVWKHIE; -.
DR   PhylomeDB; P06709; -.
DR   BioCyc; EcoCyc:BIOTINLIG-MON; -.
DR   BioCyc; MetaCyc:BIOTINLIG-MON; -.
DR   BRENDA; 6.3.4.15; 2026.
DR   EvolutionaryTrace; P06709; -.
DR   PRO; PR:P06709; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0017053; C:transcription repressor complex; IDA:CAFA.
DR   GO; GO:0005524; F:ATP binding; IMP:CAFA.
DR   GO; GO:0009374; F:biotin binding; IDA:CAFA.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IDA:EcoliWiki.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR   GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CAFA.
DR   GO; GO:0009102; P:biotin biosynthetic process; IMP:EcoliWiki.
DR   GO; GO:0006768; P:biotin metabolic process; IMP:CAFA.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd16442; BPL; 1.
DR   DisProt; DP00349; -.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00978; Bifunct_BirA; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR030855; Bifunct_BirA.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004409; Biotin_operon_repress_HTH.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50037; SSF50037; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00121; birA_ligase; 1.
DR   TIGRFAMs; TIGR00122; birA_repr_reg; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Biotin; DNA-binding; Ligase; Nucleotide-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..321
FT                   /note="Bifunctional ligase/repressor BirA"
FT                   /id="PRO_0000064932"
FT   DOMAIN          67..254
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   DNA_BIND        22..41
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT   BINDING         89..91
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT   BINDING         112
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00978,
FT                   ECO:0000269|PubMed:11353844, ECO:0000269|PubMed:1409631"
FT   BINDING         116..118
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT   BINDING         183
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00978,
FT                   ECO:0000269|PubMed:11353844, ECO:0000269|PubMed:1409631"
FT   VARIANT         61
FT                   /note="P -> A (in strain: RDD012)"
FT   VARIANT         70
FT                   /note="K -> E (in strain: RDD012)"
FT   MUTAGEN         52
FT                   /note="T->I: Does not affect repressor activity."
FT                   /evidence="ECO:0000269|PubMed:24189073"
FT   MUTAGEN         52
FT                   /note="T->S: 5-fold increase of repressor activity.
FT                   Increases binding to DNA."
FT                   /evidence="ECO:0000269|PubMed:24189073"
FT   MUTAGEN         57
FT                   /note="G->S: Lack of repressor activity. Does not bind
FT                   DNA."
FT                   /evidence="ECO:0000269|PubMed:24189073"
FT   MUTAGEN         58
FT                   /note="Y->F: Lack of repressor activity."
FT                   /evidence="ECO:0000269|PubMed:24189073"
FT   MUTAGEN         58
FT                   /note="Y->T: Does not affect repressor activity."
FT                   /evidence="ECO:0000269|PubMed:24189073"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           22..29
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           33..45
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           69..74
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:2EWN"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           96..100
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          129..139
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2EWN"
FT   HELIX           147..163
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          182..192
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:1HXD"
FT   STRAND          199..208
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:2EWN"
FT   TURN            226..230
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           235..256
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   HELIX           262..268
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   TURN            270..273
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          274..280
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          283..292
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:1HXD"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          305..311
FT                   /evidence="ECO:0007829|PDB:1BIA"
FT   STRAND          313..316
FT                   /evidence="ECO:0007829|PDB:1BIA"
SQ   SEQUENCE   321 AA;  35312 MW;  B80AEBCEEE1BD2D4 CRC64;
     MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV FTVPGKGYSL
     PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE LKSGDACIAE YQQAGRGRRG
     RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ
     DRKLAGILVE LTGKTGDAAQ IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA
     MLIRELRAAL ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL
     EQDGIIKPWM GGEISLRSAE K
 
 
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