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UniProtKB - Q05514 (MAAL_CLOTT)

Entry version 102 (02 Jun 2021)
Sequence version 1 (01 Feb 1995)
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Protein

Methylaspartate ammonia-lyase

Gene
N/A
Organism
Clostridium tetanomorphum
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-methylaspartate), L-aspartate, fumarate and ethylfumarate as substrates.

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by calcium ions.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 61 sec(-1) for amination of mesaconate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius). Kcat is 89 sec(-1) for deamination of L-threo-beta-methylaspartate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius).
  1. KM=0.65 mM for L-threo-beta-methylaspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
  2. KM=0.67 mM for L-threo-beta-methylaspartate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
  3. KM=0.7 mM for mesaconate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 Publications
  4. KM=1 mM for L-threo-beta-methylaspartate (with 20 mM of MgCl2 at pH 9 and at 30 degrees Celsius)3 Publications
  5. KM=2.3 mM for L-aspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
  6. KM=2.8 mM for L-threo-beta-methylaspartate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
  1. Vmax=2089 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 50 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
  2. Vmax=309 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 0.3 mM of KCl at pH 9 and at 30 degrees Celsius)3 Publications
  3. Vmax=266 µmol/min/mg enzyme with L-threo-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
  4. Vmax=2.5 µmol/min/mg enzyme with L-erythro-beta-methylaspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications
  5. Vmax=2.4 µmol/min/mg enzyme with L-aspartate as substrate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)3 Publications

pH dependencei

Optimum pH is 9.7.3 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius. It retains only half of its original activity after a 30 minutes incubation period at 50 degrees Celsius.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-glutamate degradation via mesaconate pathway

This protein is involved in step 2 of the subpathway that synthesizes acetate and pyruvate from L-glutamate. This subpathway is part of the pathway L-glutamate degradation via mesaconate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate and pyruvate from L-glutamate, the pathway L-glutamate degradation via mesaconate pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei172L-threo-beta-methylaspartateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei194Transition state stabilizer1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi238Magnesium2 Publications1
Metal bindingi273Magnesium2 Publications1
Metal bindingi307Magnesium2 Publications1
Binding sitei329L-threo-beta-methylaspartate1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei331Proton acceptor2 Publications1
Binding sitei361L-threo-beta-methylaspartate1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
LigandCobalamin, Cobalt, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-1103

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.3.1.2, 1527

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00561;UER00618

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Methylaspartate ammonia-lyase (EC:4.3.1.2)
Short name:
MAL
Alternative name(s):
3-methylaspartase ammonia-lyase
Beta-methylaspartase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiClostridium tetanomorphum
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1553 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Firmicutes › Clostridia › Eubacteriales › Clostridiaceae › Clostridium

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73Q → A: It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective. 1 Publication1
Mutagenesisi194H → A: Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes. 1 Publication1
Mutagenesisi194H → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi329Q → A: Very strong decrease of the catalytic efficiency for deamination, whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes. 1 Publication1
Mutagenesisi329Q → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi331K → A: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi331K → G: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi331K → H: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi331K → Q: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi331K → R: It abolishes deaminase and aminase activities and does not show any major conformational changes. 1 Publication1
Mutagenesisi384L → A: It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB03661, L-cysteic acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000845471 – 413Methylaspartate ammonia-lyaseAdd BLAST413

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

4 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q05514

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q05514

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni360 – 361L-threo-beta-methylaspartate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the methylaspartate ammonia-lyase family.Curated

Family and domain databases

Conserved Domains Database

More...CDDi		cd03314, MAL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.20.120, 1 hit
3.30.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036849, Enolase-like_C_sf
IPR029017, Enolase-like_N
IPR006395, Me_Asp_am_lyase
IPR022662, MeAsp_NH4-lyase_C
IPR022665, MeAsp_NH4-lyase_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07476, MAAL_C, 1 hit
PF05034, MAAL_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF017107, MAL, 1 hit

Structure-Function Linkage Database

More...SFLDi		SFLDF00007, methylaspartate_ammonia-lyase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51604, SSF51604, 1 hit
SSF54826, SSF54826, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01502, B_methylAsp_ase, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q05514-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG 
        60         70         80         90        100
ESISVLLVLE DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK 
       110        120        130        140        150
LIGREITNFK PMAEEFDKMT VNGNRLHTAI RYGITQAILD AVAKTRKVTM 
       160        170        180        190        200
AEVIRDEYNP GAEINAVPVF AQSGDDRYDN VDKMIIKEAD VLPHALINNV 
       210        220        230        240        250
EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY GTIGAAFDVD 
       260        270        280        290        300
IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV 
       310        320        330        340        350
DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA 
       360        370        380        390        400
NGMGAYCGGT CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN 
       410 
EMNRVLALVG RRK
Length:413
Mass (Da):45,534
Last modified:February 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4451923DB035EF13
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
S48141 Genomic DNA Translation: AAB24070.1
X70499 Genomic DNA Translation: CAA49911.1
X70695 Genomic DNA Translation: CAA50027.1

Protein sequence database of the Protein Information Resource

More...PIRi		B44285

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S48141 Genomic DNA Translation: AAB24070.1
X70499 Genomic DNA Translation: CAA49911.1
X70695 Genomic DNA Translation: CAA50027.1
PIRiB44285

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KCZX-ray1.90A/B1-413[»]
1KD0X-ray1.90A/B1-413[»]
3ZVHX-ray1.99A/B1-413[»]
3ZVIX-ray1.90A/B1-413[»]
SMRiQ05514
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB03661, L-cysteic acid

Enzyme and pathway databases

UniPathwayiUPA00561;UER00618
BioCyciMetaCyc:MONOMER-1103
BRENDAi4.3.1.2, 1527

Miscellaneous databases

EvolutionaryTraceiQ05514

Family and domain databases

CDDicd03314, MAL, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
InterProiView protein in InterPro
IPR036849, Enolase-like_C_sf
IPR029017, Enolase-like_N
IPR006395, Me_Asp_am_lyase
IPR022662, MeAsp_NH4-lyase_C
IPR022665, MeAsp_NH4-lyase_N
PfamiView protein in Pfam
PF07476, MAAL_C, 1 hit
PF05034, MAAL_N, 1 hit
PIRSFiPIRSF017107, MAL, 1 hit
SFLDiSFLDF00007, methylaspartate_ammonia-lyase, 1 hit
SUPFAMiSSF51604, SSF51604, 1 hit
SSF54826, SSF54826, 1 hit
TIGRFAMsiTIGR01502, B_methylAsp_ase, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMAAL_CLOTT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05514
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 2, 2021
This is version 102 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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