Q9KCT3

PR
Gene name
cysH
Protein name
Adenosine 5'-phosphosulfate reductase
Names
APS reductase, 5'-adenylylsulfate reductase, Thioredoxin-dependent 5'-adenylylsulfate reductase
Species
Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans)
KEGG Pathway
bha:BH1486
EC number
1.8.4.10: With a disulfide as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

182-231 (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 Q9KCT3

Entry ID Method Resolution Chain Position Source
AF-Q9KCT3-F1 Predicted AlphaFoldDB

No variants for Q9KCT3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9KCT3

No associated diseases with Q9KCT3

7 regional properties for Q9KCT3

Type Name Position InterPro Accession
domain Tetrapyrrole methylase 218 - 427 IPR000878
conserved_site Uroporphiryn-III C-methyltransferase, conserved site 221 - 235 IPR003043-1
conserved_site Uroporphiryn-III C-methyltransferase, conserved site 296 - 329 IPR003043-2
domain Uroporphyrin-III C-methyltransferase 216 - 448 IPR006366
domain Sirohaem synthase, N-terminal 4 - 203 IPR006367
domain Sirohaem synthase, dimerisation domain 150 - 207 IPR019478
domain Siroheme synthase, central domain 119 - 145 IPR028281

Functions

Description
EC Number 1.8.4.10 With a disulfide as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 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.
adenylyl-sulfate reductase (thioredoxin) activity Catalysis of the reaction: AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin.
metal ion binding Binding to a metal ion.
phosphoadenylyl-sulfate reductase (thioredoxin) activity Catalysis of the reaction: adenosine 3',5'-diphosphate + H(+) + sulfite + thioredoxin disulfide = 3'-phospho-5'-adenylyl sulfate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin; 3'-phosphoadenosine 5'-phosphosulfate is also known as PAPS.

2 GO annotations of biological process

Name Definition
cysteine biosynthetic process The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid.
sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) The pathway by which inorganic sulfate is processed and incorporated into sulfated compounds, where the phosphoadenylyl sulfate reduction step is catalyzed by the enzyme phosphoadenylyl-sulfate reductase (thioredoxin) (EC:1.8.4.8).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDQSIQVNIN EVNQALERKD SLDVIKWAYK TYGDKLVYAC SMGAEGMVLI DLISKVRPDA
70 80 90 100 110 120
PVIFLDTDFH FSETYELIER VKERYPKLQL KLVKPELTPE EQAETYGDRL WERQPDLCCK
130 140 150 160 170 180
LRKLVPLEKE LAQYDAWMSG LRRDQSPTRT NTQFVNEDRR FGSTKICPLI HWTSEEIWMY
190 200 210 220 230
IELHQLPYND LHDKQYPSIG CEYCTRPVKE GEDERAGRWS NTSKTECGLH Q