B2VL10

PR
Gene name
pqqE
Protein name
PqqA peptide cyclase
Names
Coenzyme PQQ synthesis protein E, Pyrroloquinoline quinone biosynthesis protein E
Species
Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99)
KEGG Pathway
eta:ETA_28860
EC number
1.21.98.4: With other, known acceptors
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

306-382 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B2VL10

Entry ID Method Resolution Chain Position Source
AF-B2VL10-F1 Predicted AlphaFoldDB

No variants for B2VL10

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2VL10

No associated diseases with B2VL10

4 regional properties for B2VL10

Type Name Position InterPro Accession
conserved_site MoaA/NifB/PqqE, iron-sulphur binding, conserved site 18 - 29 IPR000385
domain Elp3/MiaA/NifB-like, radical SAM core domain 12 - 215 IPR006638
domain Radical SAM 8 - 223 IPR007197
domain 4Fe4S-binding SPASM domain 245 - 310 IPR023885

Functions

Description
EC Number 1.21.98.4 With other, known acceptors
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
cyclase activity Catalysis of a ring closure reaction.
iron ion binding Binding to an iron (Fe) ion.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
S-adenosyl-L-methionine binding Binding to S-adenosyl-L-methionine.

1 GO annotations of biological process

Name Definition
pyrroloquinoline quinone biosynthetic process The chemical reactions and pathways resulting in the formation of the cofactor pyrroloquinoline quinone (PQQ); it is synthesized from a small peptide containing tyrosine and glutamic acid; these amino acids in the peptide are multiply cross-linked and the rest of the peptide is removed.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNPSESNVKP PLWLLAELTY RCPLQCPYCS NPLDFAQQEK ELSTAQWIEV FKQARAMGAV
70 80 90 100 110 120
QIGFSGGEPL VRKDLPELIR SARELGFYTN LITSGIGLTQ KKIDAFAEAG LDHIQISFQA
130 140 150 160 170 180
SDETLNAALA GSQKAFQQKL EMARAVKAHG YPMVLNFVLH RHNIDQLDRI IELCIELEAD
190 200 210 220 230 240
DVELATCQFY GWAQLNREGL LPTRDQLVRA EAVVHRYREK MAASGNLANL LFVTPDYYEE
250 260 270 280 290 300
RPKGCMGGWG AIFLSVTPEG MALPCHSARQ LPIRFPSVLE HSLQDIWFNS FGFNRYRGFD
310 320 330 340 350 360
WMPEPCRSCD EKEKDFGGCR CQAFMLTGNA DNADPVCSKS EHHGTILAAR EQANCTNIQV
370 380
NQLRFRNRAN SERVNSQLIF KG