Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

     ⌊ Family coenzyme PQQ synthesis protein E (PqqE-like)

  ⌊ FunctionalDomain Coenzyme PQQ synthesis protein E (ID 381007)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM ISS PubMed:18371220
This entry was last updated onDec. 10, 2016

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 570 490288534 WP_004184158.1 (RefSeq)
Klebsiella pneumoniae Taxon ID: 573 846738473 KMK49591.1 (Genbank) URP
Klebsiella pneumoniae Taxon ID: 573 839787686 KMI60428.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Coenzyme PQQ synthesis protein E P27507 PQQE_KLEPN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 380 | Length of Functional Domain: 378

1       10        20        30        40        50        60

MSQSKPTVNPPLWLLAELTYRCPLQCPYCSNPLDFARQDKELTTEQWIEVFRQARAMGSV
QLGFSGGEPLTRKDLPELIRAARDLGFYTNLITSGIGLTESKLDAFSEAGLDHIQISFQA
SDEVLNAALAGNKKAFQQKLAMAKAVKARDYPMVLNFVLHRHNIDQLDKIIELCIELEAD
DVELATCQFYGWAFLNREGLLPTREQIARAEQVVADYRQKMAASGNLTNLLFVTPDYYEE
RPKGCMGGWGSIFLSVTPEGTALPCHSARQLPVAFPSVLEQSLESIWYDSFGFNRYRGYD
WMPEPCRSCDEKEKDFGGCRCQAFMLTGSADNADPVCSKSPHHHKILEARREAACSDIKV
SQLQFRNRTRSQLIYQTRDL
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
22 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
26 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
29 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
22 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
26 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
29 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
22 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
26 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
29 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
306 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Function predicted based on the presence of a SPASM domain and similarity to other proteins in this subgroup 		cofactor binding -- binding IEA
309 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Function predicted based on the presence of a SPASM domain and similarity to other proteins in this subgroup 		cofactor binding -- binding IEA
319 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Function predicted based on the presence of a SPASM domain and similarity to other proteins in this subgroup 		cofactor binding -- binding IEA
321 Cys (C) side chain Binds [4Fe-4S] cluster
Notes: Function predicted based on the presence of a SPASM domain and similarity to other proteins in this subgroup 		cofactor binding -- binding IEA

Catalyzed Reaction

Tyr-Glu cyclase

+ + 2 + +
Glu-Val-Thr-Leu-Tyr peptide fragment
85622		 S-adenosyl-L-methionine zwitterion
59789		 C9-C9a linked PQQ
85623		 hydron
15378		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: 5.-.-.- | IntEnz: 5.-.-.- | Kegg: 5.-.-.- | BioCyc: 5.-.-.- | BRENDA: 5.-.-.- |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:30 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 380 378
EC number assigned by UniProtKB accession ID.