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 A9L389

Entry ID Method Resolution Chain Position Source
AF-A9L389-F1 Predicted AlphaFoldDB

No variants for A9L389

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9L389

No associated diseases with A9L389

1 regional properties for A9L389

Type Name Position InterPro Accession
domain Phosphoadenosine phosphosulphate reductase 29 - 257 IPR002500

Functions

Description
EC Number 2.7.7.4 Nucleotidyltransferases
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

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
sulfate adenylyltransferase (ATP) activity Catalysis of the reaction: ATP + sulfate = diphosphate + adenylylsulfate.

3 GO annotations of biological process

Name Definition
hydrogen sulfide biosynthetic process The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
sulfate assimilation The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.
sulfate reduction The chemical reactions and pathways resulting in the reduction of sulfate to another sulfur-containing ion or compound such as hydrogen sulfide, adenosine-phosphosulfate (APS) or thiosulfate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAGRELSHLQ QLEAESIQII REVAAEFDNP VMLYSIGKDS SVMLHLARKA FYPGKIPFPL
70 80 90 100 110 120
LHVDTGWKFK EMIAFRDAQA KKFGFELLTH INPEGLAQGI NPFDHGSAKH TDIMKTQGLK
130 140 150 160 170 180
QALNQYGFDA AFGGARRDEE KSRAKERVYS FRDRHHRWDP KNQRPELWRT YNGAVNKGES
190 200 210 220 230 240
IRVFPLSNWT ELDIWQYIYQ ENIELVPLYF AAKRQVVERG GQLIMADDER MKLAEGEQIK
250 260 270 280 290 300
EEVVRFRTLG CYPLTAAMHS EADSLEKIIE EMLLTRSSER QGRLIDSDQS ASMEQKKRQG
YF