Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B9KD35

Entry ID Method Resolution Chain Position Source
AF-B9KD35-F1 Predicted AlphaFoldDB

No variants for B9KD35

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9KD35

No associated diseases with B9KD35

3 regional properties for B9KD35

Type Name Position InterPro Accession
conserved_site ArgE/DapE/ACY1/CPG2/YscS, conserved site 60 - 69 IPR001261-1
conserved_site ArgE/DapE/ACY1/CPG2/YscS, conserved site 94 - 129 IPR001261-2
domain Peptidase M20, dimerisation domain 168 - 269 IPR011650

Functions

Description
EC Number 3.5.1.18 In linear amides
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

3 GO annotations of molecular function

Name Definition
cobalt ion binding Binding to a cobalt ion (Co).
succinyl-diaminopimelate desuccinylase activity Catalysis of the reaction: N-succinyl-LL-2,6-diaminopimelate + H(2)O = LL-2,6-diaminopimelate + succinate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
diaminopimelate biosynthetic process The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
lysine biosynthetic process via diaminopimelate The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQVVEIFKEL CKFKSITPDD DGALNYIAVE LSEFEAFFIE KEGVKNLLLT KKFSDDGEHL
70 80 90 100 110 120
AFGGHVDVVP AGEGWSNDPF EPLDKDGFIY ARGAQDMKSG VAAFMCAVKE VENFKGRISL
130 140 150 160 170 180
ILTSDEEGEA KFGTLEVLKF MKEKDILPDF AVVAEPTCDK KFGDSIKVGR RGSINAKLLI
190 200 210 220 230 240
KGKQGHVAYP QKCINPVHNF ASALKFLAGF DLDPGDEAFA PSKIVITDIR GGMEVCNVTP
250 260 270 280 290 300
NDLKLMFNVR NSPQTSLEDV KAYVEKTCEG LDYELSINQS SKPFLTQSDS KIVQKLNESV
310 320 330 340 350 360
QKITQVVPEL NTKGGTSDAR YFAEFGVKVV EFGVCNDRIH AIDERVSIEE LEKLYLVFKD
LLENFN