Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup PLP-dependent

     ⌊ Family glutamate 2,3-aminomutase

  ⌊ FunctionalDomain Glutamate 2,3-aminomutase (ID 386081)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM IES PubMed:17222594
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Desulfotomaculum reducens Taxon ID: 59610 500208254 WP_011878467.1 (RefSeq)
n/a 217271853 ACK28019.1 (Genbank)
Desulfotomaculum reducens MI-1 Taxon ID: 349161 134052694 ABO50665.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A4J6G2 A4J6G2_DESRM (TrEMBL)

Sequence

Length of Enzyme (full-length): 422 | Length of Functional Domain: 415

1       10        20        30        40        50        60

MSVHLKQEEFRLRQEKRKIALKRAKELKARITDYLENKDQIKNGFEVQEQYNRAKQTLLN
FFNADNEQWENWHWQMANRIKDVKVISQLIDLSPAEKEAIEKVGRQYRWAVSPYYMALAM
VSGSGGPVWLQAIPCIEEVKDRYGVEDPMGEEYTSPVEGVTRRYPDRLIINVTNQCAMYC
RHCQRRRNIGEIDVHKSRKVLEGALQYIRENKEIRDVLITGGDALLLSDRQIEWLLTELD
NIPHVEIKRLGTRTPVTMPQRITPELCKILENHPPIYINTQFNHPLEVTPEAKKACDMLV
KAGVVLGNQAVLLKNINNQPDVMKRLNQSLLTIRVRPYYIFHAKAVKGTRHFITGVDDGI
AIMEQLRGYTSGLAVPTYIINAPNGYGKTPVLPQYIIENKNDQVTLRTWEKRIIPYNISG
KH
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
176 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
180 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
183 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
164 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
176 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
180 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
183 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
388 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS
Family CAR This EFD conserves 10/10 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
164 Tyr (Y) side chain PLP binding
Notes: PLP enzymes require a bulky aromatic or aliphatic residue that prevents the cofactor from moving in the active site once it has been released from the covalent attachment to the enzyme during the course of the reaction. 		cofactor binding -- binding IEA
167 Arg (R) side chain PLP binding cofactor binding -- binding IEA
176 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
180 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
183 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
187 Arg (R) side chain Binds glutamate substrate substrate binding -- binding IEA
249 Arg (R) side chain PLP binding cofactor binding -- binding IEA
344 Lys (K) side chain Binds glutamate substrate substrate binding -- binding ISS
381 Asn (N) side chain Binds glutamate substrate substrate binding -- binding ISS
388 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS

Catalyzed Reaction

glutamate 2,3-aminomutase

L-glutamate(1-)
29985		 isoglutamate(1-)
66948

EC: 5.4.3.9 | IntEnz: 5.4.3.9 | Kegg: 5.4.3.9 | BioCyc: 5.4.3.9 | BRENDA: 5.4.3.9

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:31 a.m. update curation agent holliday setDomainBoundaries.py
update domain start position 1 7
EC number assigned by UniProtKB accession ID.