Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

     ⌊ Family cytosylglucuronate decarboxylase

  ⌊ FunctionalDomain cytosylglucuronate decarboxylase (BlsE) (ID 434548)

Superfamily Assignment Evidence Code(s) ISS PubMed:23874663
Family Assignment Evidence Code CFM PubMed:23874663
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces griseochromogenes Taxon ID: 68214 29899152 AAP03119.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q841K9 Q841K9_9ACTN (TrEMBL)

Sequence

Length of Enzyme (full-length): 344 | Length of Functional Domain: 332

1       10        20        30        40        50        60

MTERTASRPSGPGRRGSTRERYLFIRLLEACNADCFMCDFALSRDTFRFSLEDFDELLPR
AVEAGVGYIRFTGGEPLMHTDVAELVRRGTDAGMKMSIITNGMMLPRQIERLADAGLAQI
IVSLDGGSAATHDVYRRSPGMFDNGLRGLRAAARLGVLPRVNSVVGPHNYTEMPQLQRVL
TEAGVRQWELSALKLERAISYPDPDHVRALCDPVYDADPEHMLVPLGKRFYGDTPEEQEL
YFSDSVTPRASAPLCHVVDDVIYLDGKYGRAYACSCLPHREGDDEPGGAPLREDGVIRLD
TPAFRTHADFFRTEGPCVCNGCSTTAAGYSDDIARLGGVRPWQY
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
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
35 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
38 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
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
35 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
38 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
35 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
38 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
255 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
274 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA
276 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IEA

Catalyzed Reaction

cytosylglucuronate decarboxylase

+ + + +
cytosylglucuronate
132252		 S-adenosyl-L-methionine zwitterion
59789		 cytosylarabinopyranose
132134		 carbon dioxide
16526		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

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

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:20 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 237 196
Oct. 15, 2016, 7:04 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update domain end position 196 344
update name cytosylglucuronic acid decarboxylase (BlsE) cytosylglucuronate decarboxylase (BlsE)
update domain start position 3 13
EC number assigned by UniProtKB accession ID.