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 Q8UAA9

Entry ID Method Resolution Chain Position Source
AF-Q8UAA9-F1 Predicted AlphaFoldDB

No variants for Q8UAA9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8UAA9

No associated diseases with Q8UAA9

3 regional properties for Q8UAA9

Type Name Position InterPro Accession
domain Metallo-beta-lactamase 156 - 345 IPR001279
domain Beta-lactamase hydrolase-like protein, phosphatase-like domain 4 - 132 IPR005939
domain Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain 146 - 347 IPR044528

Functions

Description
EC Number
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
hydrolase activity, acting on ester bonds Catalysis of the hydrolysis of any ester bond.
metal ion binding Binding to a metal ion.
sulfur dioxygenase activity Catalysis of the reaction: sulfur + O2 + H2O = sulfite.

1 GO annotations of biological process

Name Definition
glutathione metabolic process The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKAVRINERL TIAGQPMIAD FPSLSAQGFK SIINARPDGE EPGQPGNTQE KSAAGAAGMD
70 80 90 100 110 120
YGFIPVSGPT ITEADIRAFQ QKMAEAEGPV FAHCKGGTRA LTLYVLGEAL DGRIQRSDIE
130 140 150 160 170 180
DFGKTHGFDL CAATRWLERQ SAAVPHIKAF FDPRTWSVQY VVSDPATGGC AIIDPVYDFD
190 200 210 220 230 240
EKSGATGTMN ADAILDYVKR HGLSVEWILD THPHADHFSA ADYLKQKTGA KTAIGAKVTG
250 260 270 280 290 300
VQKLWQEKYN WSDFKTDGSQ WDQLFEAGDR FSIGSLEARV LFSPGHTLAS VTYVVGNAAF
310 320 330 340 350 360
VHDTLFMPDS GTARADFPGG SAKQLWASIQ DILALPDDTR LFTGHDYQPG GRAPKWESTV
370 380 390 400 410 420
GEQTRSNPHL AGMTEEDFVR LREARDRTLP MPKLILHALQ VNIRGGRLPE PEANGKHYLK
430
FPLDVLEGST W