Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ cleavage of the Ca-Cb bond in aromatic amino acids

     ⌊ Family 2-iminoacetate synthase (ThiH)

  ⌊ FunctionalDomain 2-iminoacetate synthase (ID 280101)

Superfamily Assignment Evidence Code(s) ISS PubMed:17969213 PubMed:17403671
Family Assignment Evidence Code CFM PubMed:17969213 PubMed:17403671
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16131820 NP_418417.1 (RefSeq) URP
Taxon ID: 543 446770191 WP_000847447.1 (RefSeq)
Escherichia coli Taxon ID: 562 857138672 AKO55139.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
2-iminoacetate synthase P30140 THIH_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 377 | Length of Functional Domain: 373

1       10        20        30        40        50        60

MKTFSDRWRQLDWDDIRLRINGKTAADVERALNASQLTRDDMMALLSPAASGYLEQLAQR
AQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNRIKRKTLDEADIARESAAIREM
GFEHLLLVTGEHQAKVGMDYFRRHLPALREQFSSLQMEVQPLAETEYAELKQLGLDGVMV
YQETYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDNWRVDSYMVA
EHLLWLQQHYWQSRYSVSFPRLRPCTGGIEPASIMDERQLVQTICAFRLLAPEIELSLST
RESPWFRDRVIPLAINNVSAFSKTQPGGYADNHPELEQFSPHDDRRPEAVAAALTAQGLQ
PVWKDWDSYLGRASQRL
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
85 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
89 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
92 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
85 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
89 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
92 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
85 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
89 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
92 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
102 Arg (R) side chain Unknown -- IMP PubMed:15271986
338 Gln (Q) side chain Unknown -- IMP PubMed:15271986

Catalyzed Reaction

2-iminoacetate synthase

+ + + + + +
S-adenosyl-L-methionine zwitterion
59789		 L-tyrosine zwitterion
58315		 NADPH(4-)
57783		 dehydroglycine zwitterion
77846		 p-cresol
17847		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844		 NADP(3-)
58349

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

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 377 373
May 11, 2015, 8:44 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code CFM,IES CFM
EC number assigned by UniProtKB accession ID.