B4LRB9

PR
Gene name
Uba4
Protein name
Adenylyltransferase and sulfurtransferase MOCS3
Names
Molybdenum cofactor synthesis protein 3, Ubiquitin activating enzyme 4
Species
Drosophila virilis (Fruit fly)
KEGG Pathway
dvi:6628147
EC number
2.7.7.80: Nucleotidyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-89 (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 B4LRB9

Entry ID Method Resolution Chain Position Source
AF-B4LRB9-F1 Predicted AlphaFoldDB

No variants for B4LRB9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B4LRB9

No associated diseases with B4LRB9

2 regional properties for B4LRB9

Type Name Position InterPro Accession
domain THIF-type NAD/FAD binding fold 70 - 307 IPR000594
domain Rhodanese-like domain 344 - 450 IPR001763

Functions

Description
EC Number 2.7.7.80 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
molybdopterin synthase complex A protein complex that possesses molybdopterin synthase activity. In E. coli, the complex is a heterotetramer consisting of two MoaD and two MoaE subunits.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
molybdopterin-synthase adenylyltransferase activity Catalysis of the reaction: ATP
molybdopterin-synthase sulfurtransferase activity Catalysis of the reaction: -Gly-NH-CH(2)-C(O)SH + cysteine desulfurase.
thiosulfate sulfurtransferase activity Catalysis of the reaction: hydrogen cyanide + thiosulfate = H(+) + sulfite + thiocyanate.
ubiquitin-like modifier activating enzyme activity Catalysis of the activation of small proteins, such as ubiquitin or ubiquitin-like proteins, through the formation of an ATP-dependent high-energy thiolester bond.

4 GO annotations of biological process

Name Definition
Mo-molybdopterin cofactor biosynthetic process The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
molybdopterin cofactor biosynthetic process The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
protein urmylation Covalent attachment of the ubiquitin-like protein URM1 to another protein.
tRNA wobble position uridine thiolation The process in which a uridine residue at position 34 in the anticodon of a tRNA is post-transcriptionally thiolated at the C2 position. This process involves transfer of a sulfur from cysteine to position C2 by several steps.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIAAANCLET EKAKLRREIA ELQAALNAKE QNLRDLQSRT AASHLDPEAD LQHATREQYA
70 80 90 100 110 120
TLNNDDIARY SRQLILSDFG VSGQLKLKNS AVLIVGLGGL GCPAAQYLCS AGCGNLGLVD
130 140 150 160 170 180
YDEVERSNLH RQTLHTVARC GMSKTESARI ALLELNPHCR ITCYPRLLNS SNAMHIMRAY
190 200 210 220 230 240
DIVLDCSDNV ATRYLLNDAC TMLRKPLVSG SALKLDGQLT VYSYGAQGPC YRCIYPVPPP
250 260 270 280 290 300
PEAVTNCGDG GVLGAVTGTI GAMQALEAIK IIIGLGDVLA GRMLIFDGSS CQFRNIKIRS
310 320 330 340 350 360
KRPNCHVCSA QPLITGLIDY ELFCGMNAND KDNAVKLLEP EERINVLDYQ RLMKTKAHLL
370 380 390 400 410 420
LDVRAPAEFE ICQLPDSINV PLAHVLDDSY LQRFAQQLES KELPIFVVCR RGNDSQIAVQ
430 440 450
HMRTRLPEHS IRDLEGGLHA WTNQVDQSFP IY