Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup PLP-dependent

     ⌊ Family arginine 2,3-aminomutase

  ⌊ FunctionalDomain Arginine aminomutase (ID 386084)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:12964155
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces griseochromogenes Taxon ID: 68214 29899154 AAP03121.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q841K7 Q841K7_9ACTN (TrEMBL)

Sequence

Length of Enzyme (full-length): 410 | Length of Functional Domain: 373

1       10        20        30        40        50        60

MSHMSTESDGIRPSLTRREDIPDEQWNDWRWHMRKRITNLDKAREWIRPTPLEEKAIAET
AGKYRWSVTPYYASLMDPDDPGCPVRQQAVPALGELMEFSGAEVDPVGDMYYRRTNRVVH
KYPDRVIMLITEACPVYCRHCTRKFHTTDVDGTYFERNEGEDFSEDLRYIADHPEIRDVL
LTGGDPLSYRDGKLEEIIAGLRAIPSVEIIRIGSRFPVLLPQRVTPELCEMLARYHPVWL
NTHFNHPKEITPESERAIDRLLRHGIPVGNQTVLLRGINDDLGTMRRLMTELLRIRVRPY
YLYHCDNVTGVSHFMTSVEKGWEIMEGLQGHITGFGVPQYVLTTRLGKIPMVRPYYRETP
DGLVLRNYRGEEMLVDDSVCPLTESAAAHAFRNAPDVTENRTTATGEGAR
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
134 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
138 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
141 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
122 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
134 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
138 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
141 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
348 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
122 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
125 Arg (R) side chain PLP binding cofactor binding -- binding IEA
134 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
138 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
141 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
211 Arg (R) side chain PLP binding cofactor binding -- binding IEA
348 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS

Catalyzed Reaction

arginine 2,3-aminomutase

L-argininium(1+)
32682		 isoarginine
85624

EC: 5.4.3.- | IntEnz: 5.4.3.- | Kegg: 5.4.3.- | BioCyc: 5.4.3.- | BRENDA: 5.4.3.- |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:31 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 390 384
update domain start position 14 12
EC number assigned by UniProtKB accession ID.