Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup B12-binding domain containing

     ⌊ Family   private

  ⌊ FunctionalDomain SanA (ID 435041)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:27642865
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces ansochromogenes Taxon ID: 115647 7341211 AAF61217.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q9L7A0 Q9L7A0_9ACTN (TrEMBL)

Sequence

Length of Enzyme (full-length): 454 | Length of Functional Domain: 454

1       10        20        30        40        50        60

MGKIVDEPRKILVIWPPQVLSYFNAGHHLALYQVTGHLRAVYPGAQVTAIDASVERLTWK
DLGSRLFQERYDVIAVMNEFDGIDGLRRLVSYARALNPDAPIVTFGRLSGVNPRFFERFD
IDAIVENGDFESGVVAAIEAFRGRAADAAGVHLRRDGSWAAPKRRGDLLPAEDWYLPTPD
EIPYGHYDALYFDDANKFCGIPRRRELVVPAARGCPVGCSYCEVPLIYTRKERRLTVERT
VRYIEESFAAAPFEYVAFYAPTFTLDKKWTKELCRELTGRGSPYPWKCATTVHHLGEGMI
RSMGAAGCVRISVGLETLDPQEGRVAAPGEEKSATDLDRLSAWCEESGIELNCFVIVGLP
GTTIEGAERTIEAVQQRGGRARPTVYAPWELAGPDLPDHEMAAFNRQLFVPGTHALTDDE
LARGYDIVFGSQPDVTQVFENIPARAAGPALRPA
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
215 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
219 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
222 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
215 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
219 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
222 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 4/4 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
199 Cys (C) side chain Radical acceptor/donor single electron shuttle -- reactant IMP PubMed:27642865
215 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:27642865
219 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:27642865
222 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:27642865

Catalyzed Reaction

EP-UMP cyclase

+ + +
EP-UMP
133864		 S-adenosyl-L-methionine zwitterion
59789		 U-OAP
133866		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319

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 418 429
update domain start position 3 2
Oct. 15, 2016, 7:06 a.m. update domain end position 429 434
update domain start position 2 9
Dec. 14, 2016, 6:58 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update domain end position 434 454
update name Magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase SanA
update domain start position 9 1
EC number assigned by UniProtKB accession ID.