6.2.1.45: E1 ubiquitin-activating enzyme

This is an abbreviated version!
For detailed information about E1 ubiquitin-activating enzyme, go to the full flat file.

Reaction

Synonyms

AtUBA1, AtUBA2, E1, E1 ubiquitin-activating enzyme, HsUba1a, non-canonical ubiquitin activating enzyme, SUMO E1, UB activating enzyme, Ub E1 activating enzyme, Ub-activating enzyme, Ub-activating ligase, Uba1, Uba1/E1, Uba1a, UBA1p, UBA2, UBA5, Uba6, UBA7, UBE1, UBE1DC1, UBE1DC1A, UBE1DC1B, UBE1L, UBE1L2, ubiquitin activating enzyme, ubiquitin activating enzyme 2, ubiquitin activating enzyme E1, ubiquitin activating enzyme E1-like, ubiquitin E1, ubiquitin protein ligase E1, Ubiquitin-activating enzyme, ubiquitin-activating enzyme (E1), ubiquitin-activating enzyme 1, ubiquitin-activating enzyme 5, ubiquitin-activating enzyme 6, ubiquitin-activating enzyme E1, ubiquitin-activating enzyme E1 domain-containing protein 1, ubiquitin-activating enzyme E1-domain containing 1, ubiquitin-activating enzyme, UBE1, ubiquitin-conjugating enzyme, ubiquitin-like modifier-activating enzyme 1, ubiquitin-like modifier-activating enzyme 5, ubiquitin-like modifier-activating enzyme 6, ubiquitin-like modifier-activating enzyme 7 isoform X2

ECTree

     6 Ligases

         6.2 Forming carbon-sulfur bonds

             6.2.1 Acid-thiol ligases

                6.2.1.45 E1 ubiquitin-activating enzyme

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
4	Activating Compound
2393	AA Sequence
7	Application
31	Cloned(Commentary)
16	Cofactor
7	Crystallization (Commentary)
861	Disease/ Diagnostics
4	Expression
43	General Information
3	IC50 Value
27	Inhibitors
1	Ki Value [mM]
28	KM Value [mM]
11	Localization
17	Metals/Ions
16	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
52	Organism
1	Pathway
42	PDB ID
7	pH Optimum
1	pI Value
3	Posttranslational Modification
33	Protein Variants
16	Purification (Commentary)
5	Reaction
49	Reference
62	Source Tissue
2	Storage Stability
55	Substrates and Products (Substrate)
16	Subunits
100	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
30	Turnover Number [1/s]

Subunits

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Subunits on EC 6.2.1.45 - E1 ubiquitin-activating enzyme

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Subunit Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

?

6 entries

dimer

4 entries

homodimer

Homo sapiens

Q9GZZ9

dimerization of UBA5 is required for UFM1 activation. The active site Cys of UBA5 (Cys 250) is located within the adenylation domain

744655

monomer

2 entries

additional information

5 entries

?

Arabidopsis thaliana

P92974, P93028

x * 12000 and x * 124000, SDS-PAGE, x * 119600, calculated

1111

?

Arabidopsis thaliana

P92974, P93028

x * 123000, SDS-PAGE, x * 120300, calculated

1111

?

Citrus reticulata

-

x * 49280, sequence calculation

733931

?

Homo sapiens

Q712V1

x * 117000, SDS-PAGE

709881

?

Homo sapiens

P22314

x * 110450, calculated

1115

?

Homo sapiens

-

x * 42000, recombinant mRFP-enzyme, SDS-PAGE

734395

dimer

Giardia intestinalis

A8BBP6

1 * 68000 + 1 * 47000, the enzyme is proteolytically processed mainly into two fragments of 68 kDa (N-terminal) and 47 kDa (C-terminal)

733043

dimer

Giardia intestinalis ATCC 50803

-

1 * 68000 + 1 * 47000, the enzyme is proteolytically processed mainly into two fragments of 68 kDa (N-terminal) and 47 kDa (C-terminal)

-

dimer

Homo sapiens

Q9GZZ9

analytical ultracentrifugation

709113

dimer

Homo sapiens

Q9GZZ9

analytical ultracentrifugation analysis, forms primarily dimers with 1.85:1 dimers to monomers ratio

709113

monomer

Homo sapiens

Q9GZZ9

analytical ultracentrifugation analysis, forms primarily dimers with 1.85:1 dimers to monomers ratio

709113

monomer

Homo sapiens

-

1 * 117300, calculated

728208

additional information

Homo sapiens

P22314

the enzyme N-terminal domains contain inactive adenylation domain (IAD) and the first catalytic cysteine half-domain (FCCH). The IAD domain covers from Met1 to Glu204 and Val295 to Ile439 and that the FCCH domain covers from Glu205 to Gln294. The structure of ubiquitin E1 consists of four different domain blocks, overview. The enzyme forms a pseudo-dimer

733532

additional information

Homo sapiens

-

the enzyme N-terminal domains contain inactive adenylation domain (IAD) and the first catalytic cysteine half-domain (FCCH). The IAD domain covers from Met1 to Glu204 and Val295 to Ile439 and that the FCCH domain covers from Glu205 to Gln294. The structure of ubiquitin E1 consists of four different domain blocks, overview. The enzyme forms a pseudo-dimer

733532

additional information

Saccharomyces cerevisiae

P22515

the structure of E1 is organised into six domains namely, inactive adenylation domain (IAD), first catalytic cysteine half-domain (FCCH), four-helix bundles (4HB), active adenylation domain (AAD), second catalytic cysteine half-domain (SCCH) and Ub fold domain (UFD). E1 displays complex architecture due to the discontinuous and interspersed organisation of its six domains. The domains carrying the catalytic cysteine exist as two parts namely, FCCH and SCCH, which are found inserted into each of the adenylation domains. SCCH domain consisting of catalytic cysteine forms a thioester bond with ubiquitin. On the other hand FCCH, which associates with IAD is non-functional. 4HB domain present immediately after the FCCH, represents the second insertion in the IAD. UFD present in the C-terminus of E1 has a role in the recruitment of specific E2s to the ubiquitination pathway. Secondary structure analysis of enzyme domains, overview

760825

additional information

Saccharomyces cerevisiae

-

the structure of E1 is organised into six domains namely, inactive adenylation domain (IAD), first catalytic cysteine half-domain (FCCH), four-helix bundles (4HB), active adenylation domain (AAD), second catalytic cysteine half-domain (SCCH) and Ub fold domain (UFD). E1 displays complex architecture due to the discontinuous and interspersed organisation of its six domains. The domains carrying the catalytic cysteine exist as two parts namely, FCCH and SCCH, which are found inserted into each of the adenylation domains. SCCH domain consisting of catalytic cysteine forms a thioester bond with ubiquitin. On the other hand FCCH, which associates with IAD is non-functional. 4HB domain present immediately after the FCCH, represents the second insertion in the IAD. UFD present in the C-terminus of E1 has a role in the recruitment of specific E2s to the ubiquitination pathway. Secondary structure analysis of enzyme domains, overview

760825

additional information

Saccharomyces cerevisiae ATCC 204508

-

the structure of E1 is organised into six domains namely, inactive adenylation domain (IAD), first catalytic cysteine half-domain (FCCH), four-helix bundles (4HB), active adenylation domain (AAD), second catalytic cysteine half-domain (SCCH) and Ub fold domain (UFD). E1 displays complex architecture due to the discontinuous and interspersed organisation of its six domains. The domains carrying the catalytic cysteine exist as two parts namely, FCCH and SCCH, which are found inserted into each of the adenylation domains. SCCH domain consisting of catalytic cysteine forms a thioester bond with ubiquitin. On the other hand FCCH, which associates with IAD is non-functional. 4HB domain present immediately after the FCCH, represents the second insertion in the IAD. UFD present in the C-terminus of E1 has a role in the recruitment of specific E2s to the ubiquitination pathway. Secondary structure analysis of enzyme domains, overview

-