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P0AEK4

- FABI_ECOLI

UniProt

P0AEK4 - FABI_ECOLI

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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene
fabI, envM, b1288, JW1281
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.3 Publications

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.1 Publication

Enzyme regulationi

Inhibited by diazaborines, triclosan (5-chloro-2-2,4-dichlorophenoxyphenol), 1,4-disubstituted imidazoles, 1,4-benzodiazepine derivatives, naphthyridinone derivatives, luteolin and curcumin.9 Publications

Kineticsi

  1. KM=3.3 µM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius and pH 8)2 Publications
  2. KM=22 µM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5)
  3. KM=24 µM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius and pH 8)
  4. KM=2700 µM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131NAD; via carbonyl oxygen
Binding sitei40 – 401NAD
Binding sitei92 – 921NAD; via carbonyl oxygen
Binding sitei95 – 951Substrate; via amide nitrogen and carbonyl oxygen
Active sitei146 – 1461Proton acceptor By similarity
Active sitei156 – 1561Proton acceptor By similarity
Binding sitei163 – 1631NAD
Sitei201 – 2011Involved in acyl-ACP binding
Sitei204 – 2041Involved in acyl-ACP binding
Sitei205 – 2051Involved in acyl-ACP binding

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NAD
Nucleotide bindingi64 – 652NAD
Nucleotide bindingi192 – 1965NAD

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB
  2. identical protein binding Source: EcoCyc

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB
  2. fatty acid elongation Source: UniProtKB
  3. lipid biosynthetic process Source: EcoCyc
  4. protein homotetramerization Source: UniProtKB
  5. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
ECOL316407:JW1281-MONOMER.
MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
SABIO-RKP0AEK4.
UniPathwayiUPA00078.
UPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
Short name:
ENR
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene namesi
Name:fabI
Synonyms:envM
Ordered Locus Names:b1288, JW1281
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11528. fabI.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931G → S: Diazaborine resistance. 2 Publications
Mutagenesisi93 – 931G → V: Triclosan resistance. 2 Publications
Mutagenesisi146 – 1461Y → F: Large impact on catalysis, with kcat and kcat/Km for DD-ACP decreasing by around 50-fold compared with wild-type. 1 Publication
Mutagenesisi156 – 1561Y → F: No effect on substrate reduction. 1 Publication
Mutagenesisi159 – 1591M → T: Triclosan resistance. 1 Publication
Mutagenesisi201 – 2011K → A: No effect on substrate reduction. 1 Publication
Mutagenesisi201 – 2011K → E: Little activity toward DD-CoA and DD-ACP. 1 Publication
Mutagenesisi203 – 2031F → L: Triclosan resistance. 1 Publication
Mutagenesisi204 – 2041R → A: No effect on substrate reduction. 1 Publication
Mutagenesisi204 – 2041R → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. 1 Publication
Mutagenesisi205 – 2051K → A: No effect on substrate reduction. 1 Publication
Mutagenesisi205 – 2051K → E: Causes a further reduction in kcat/Km for reduction of DD-ACP without affecting kcat/Km for the DD-CoA substrate. Has a larger impact on substrate reduction. 1 Publication
Mutagenesisi241 – 2411S → F: Produces temperature-sensitive phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054899Add
BLAST

Proteomic databases

PaxDbiP0AEK4.
PRIDEiP0AEK4.

2D gel databases

SWISS-2DPAGEP0AEK4.

Expressioni

Gene expression databases

GenevestigatoriP0AEK4.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Protein-protein interaction databases

DIPiDIP-31867N.
IntActiP0AEK4. 12 interactions.
MINTiMINT-1251203.
STRINGi511145.b1288.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64
Beta strandi8 – 114
Beta strandi16 – 194
Helixi20 – 3011
Beta strandi34 – 418
Turni42 – 443
Helixi45 – 5410
Beta strandi60 – 623
Helixi68 – 7912
Beta strandi83 – 908
Helixi97 – 1004
Beta strandi101 – 1033
Helixi104 – 1074
Helixi110 – 12011
Helixi122 – 13110
Helixi132 – 1343
Beta strandi135 – 14511
Helixi147 – 1493
Turni154 – 1574
Helixi158 – 17720
Turni178 – 1814
Beta strandi182 – 1898
Helixi197 – 1993
Beta strandi200 – 2023
Helixi203 – 21311
Helixi222 – 23211
Helixi235 – 2373
Beta strandi244 – 2485
Helixi251 – 2533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C14X-ray2.00A/B1-262[»]
1D8AX-ray2.20A/B2-262[»]
1DFGX-ray2.50A/B2-262[»]
1DFHX-ray2.20A/B2-262[»]
1DFIX-ray2.09A/B/C/D2-262[»]
1I2ZX-ray2.80A/B1-262[»]
1I30X-ray2.40A/B1-262[»]
1LX6X-ray2.40A/B1-262[»]
1LXCX-ray2.40A/B1-262[»]
1MFPX-ray2.33A/B1-262[»]
1QG6X-ray1.90A/B/C/D2-262[»]
1QSGX-ray1.75A/B/C/D/E/F/G/H1-262[»]
2FHSX-ray2.70A/B1-262[»]
3PJDX-ray2.50A/B1-262[»]
3PJEX-ray2.50A/B1-262[»]
3PJFX-ray1.90A/B1-262[»]
4JQCX-ray2.80A/B1-262[»]
4JX8X-ray3.20A/B1-262[»]
ProteinModelPortaliP0AEK4.

Miscellaneous databases

EvolutionaryTraceiP0AEK4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
KOiK00208.
OMAiKLSIAWA.
OrthoDBiEOG6HF644.
PhylomeDBiP0AEK4.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEK4-1 [UniParc]FASTAAdd to Basket

« Hide

MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE    50
FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL 100
DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE 150
RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI 200
KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG 250
FSIAAMNELE LK 262
Length:262
Mass (Da):27,864
Last modified:January 23, 2007 - v2
Checksum:i436A89AF349D1866
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97219 Unassigned DNA. Translation: AAA17755.1.
X78733 Genomic DNA. Translation: CAA55381.1.
U00096 Genomic DNA. Translation: AAC74370.1.
AP009048 Genomic DNA. Translation: BAA14841.1.
PIRiS48029.
RefSeqiNP_415804.1. NC_000913.3.
YP_489556.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74370; AAC74370; b1288.
BAA14841; BAA14841; BAA14841.
GeneIDi12931141.
945870.
KEGGiecj:Y75_p1263.
eco:b1288.
PATRICi32117844. VBIEscCol129921_1342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97219 Unassigned DNA. Translation: AAA17755.1 .
X78733 Genomic DNA. Translation: CAA55381.1 .
U00096 Genomic DNA. Translation: AAC74370.1 .
AP009048 Genomic DNA. Translation: BAA14841.1 .
PIRi S48029.
RefSeqi NP_415804.1. NC_000913.3.
YP_489556.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C14 X-ray 2.00 A/B 1-262 [» ]
1D8A X-ray 2.20 A/B 2-262 [» ]
1DFG X-ray 2.50 A/B 2-262 [» ]
1DFH X-ray 2.20 A/B 2-262 [» ]
1DFI X-ray 2.09 A/B/C/D 2-262 [» ]
1I2Z X-ray 2.80 A/B 1-262 [» ]
1I30 X-ray 2.40 A/B 1-262 [» ]
1LX6 X-ray 2.40 A/B 1-262 [» ]
1LXC X-ray 2.40 A/B 1-262 [» ]
1MFP X-ray 2.33 A/B 1-262 [» ]
1QG6 X-ray 1.90 A/B/C/D 2-262 [» ]
1QSG X-ray 1.75 A/B/C/D/E/F/G/H 1-262 [» ]
2FHS X-ray 2.70 A/B 1-262 [» ]
3PJD X-ray 2.50 A/B 1-262 [» ]
3PJE X-ray 2.50 A/B 1-262 [» ]
3PJF X-ray 1.90 A/B 1-262 [» ]
4JQC X-ray 2.80 A/B 1-262 [» ]
4JX8 X-ray 3.20 A/B 1-262 [» ]
ProteinModelPortali P0AEK4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31867N.
IntActi P0AEK4. 12 interactions.
MINTi MINT-1251203.
STRINGi 511145.b1288.

Chemistry

BindingDBi P0AEK4.
ChEMBLi CHEMBL1857.

2D gel databases

SWISS-2DPAGE P0AEK4.

Proteomic databases

PaxDbi P0AEK4.
PRIDEi P0AEK4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74370 ; AAC74370 ; b1288 .
BAA14841 ; BAA14841 ; BAA14841 .
GeneIDi 12931141.
945870.
KEGGi ecj:Y75_p1263.
eco:b1288.
PATRICi 32117844. VBIEscCol129921_1342.

Organism-specific databases

EchoBASEi EB1490.
EcoGenei EG11528. fabI.

Phylogenomic databases

eggNOGi COG0623.
KOi K00208.
OMAi KLSIAWA.
OrthoDBi EOG6HF644.
PhylomeDBi P0AEK4.

Enzyme and pathway databases

UniPathwayi UPA00078 .
UPA00094 .
BioCyci EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
ECOL316407:JW1281-MONOMER.
MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER.
SABIO-RK P0AEK4.

Miscellaneous databases

EvolutionaryTracei P0AEK4.
PROi P0AEK4.

Gene expression databases

Genevestigatori P0AEK4.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequences of the envM gene and of two mutated alleles in Escherichia coli."
    Bergler H., Hoegenauer G., Turnowsky F.
    J. Gen. Microbiol. 138:2093-2100(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, MUTAGENESIS OF GLY-93.
  2. "The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes."
    Kater M.M., Koningstein G.M., Nijkamp H.J.J., Stuitje A.R.
    Plant Mol. Biol. 25:771-790(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli."
    Bergler H., Wallner P., Ebeling A., Leitinger B., Fuchsbichler S., Aschauer H., Kollenz G., Hoegenauer G., Turnowsky F.
    J. Biol. Chem. 269:5493-5496(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN ENOYL-ACP REDUCTASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
    Heath R.J., Rock C.O.
    J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS.
  10. Cited for: ENZYME REGULATION, MUTAGENESIS OF GLY-93; MET-159 AND PHE-203.
  11. "Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli from Chinese medicine monomers."
    Yao J., Zhang Q., Min J., He J., Yu Z.
    Bioorg. Med. Chem. Lett. 20:56-59(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. "Biotin synthesis begins by hijacking the fatty acid synthetic pathway."
    Lin S., Hanson R.E., Cronan J.E.
    Nat. Chem. Biol. 6:682-688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BIOTIN BIOSYNTHESIS.
  13. "A mechanism of drug action revealed by structural studies of enoyl reductase."
    Baldock C., Rafferty J.B., Sedelnikova S.E., Baker P.J., Stuitje A.R., Slabas A.R., Hawkes T.R., Rice D.W.
    Science 274:2107-2110(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
  14. "Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan."
    Ward W.H., Holdgate G.A., Rowsell S., McLean E.G., Pauptit R.A., Clayton E., Nichols W.W., Colls J.G., Minshull C.A., Jude D.A., Mistry A., Timms D., Camble R., Hales N.J., Britton C.J., Taylor I.W.
    Biochemistry 38:12514-12525(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
  15. "Structural basis and mechanism of enoyl reductase inhibition by triclosan."
    Stewart M.J., Parikh S., Xiao G., Tonge P.J., Kisker C.
    J. Mol. Biol. 290:859-865(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR.
  17. "Molecular basis for triclosan activity involves a flipping loop in the active site."
    Qiu X., Janson C.A., Court R.I., Smyth M.G., Payne D.J., Abdel-Meguid S.S.
    Protein Sci. 8:2529-2532(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR.
  18. "1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI)."
    Heerding D.A., Chan G., DeWolf W.E., Fosberry A.P., Janson C.A., Jaworski D.D., McManus E., Miller W.H., Moore T.D., Payne D.J., Qiu X., Rittenhouse S.F., Slater-Radosti C., Smith W., Takata D.T., Vaidya K.S., Yuan C.C., Huffman W.F.
    Bioorg. Med. Chem. Lett. 11:2061-2065(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
  19. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION.
  21. "Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli."
    Rafi S., Novichenok P., Kolappan S., Zhang X., Stratton C.F., Rawat R., Kisker C., Simmerling C., Tonge P.J.
    J. Biol. Chem. 281:39285-39293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), MUTAGENESIS OF TYR-146; TYR-156; LYS-201; ARG-204 AND LYS-205, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiFABI_ECOLI
AccessioniPrimary (citable) accession number: P0AEK4
Secondary accession number(s): P29132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The antibiotic diazaborine interferes with the activity by binding to the protein and NAD.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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