O59667

PR
Gene name
his7
Protein name
Histidine biosynthesis bifunctional protein his7
Names
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPBC29A3.02c
EC number
3.5.4.19: In cyclic amidines
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

145-220 (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 O59667

Entry ID Method Resolution Chain Position Source
AF-O59667-F1 Predicted AlphaFoldDB

No variants for O59667

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O59667

No associated diseases with O59667

1 regional properties for O59667

Type Name Position InterPro Accession
domain Phosphoribosyl-AMP cyclohydrolase domain 226 - 297 IPR002496

Functions

Description
EC Number 3.5.4.19 In cyclic amidines
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.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

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.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
phosphoribosyl-AMP cyclohydrolase activity Catalysis of the reaction: 1-(5-phosphonatoribosyl)-5'-AMP + H(2)O = 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide.
phosphoribosyl-ATP diphosphatase activity Catalysis of the reaction: 1-(5-phospho-D-ribosyl)-ATP + H(2)O = 1-(5-phosphonatoribosyl)-5'-AMP + diphosphate + H(+).

1 GO annotations of biological process

Name Definition
histidine biosynthetic process The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MALLPFFDLT NFESDASEEL GWLKYVGRVQ TRVFPQHFKD NLEKVRKISE TIDVIVDTTA
70 80 90 100 110 120
ELGPEACVNL LNAGALAILV NEEMLNELAD ISPNRLVLKT DTTDIGKIEK LSQVAGSIQW
130 140 150 160 170 180
IGSAENYPPD FFERASKIIH KAVMPEGGGR TLYLEFPEQP SMEVLKSFSV HSVVPVLSSS
190 200 210 220 230 240
FLTVKPAEEP KKLSLADLIL ISANTDREDG LFSTLVVNEL GIALGLVYSS KESVAESLKT
250 260 270 280 290 300
GTGVYQSRKR GLWYKGASSG AVQHLIHIDV DCDEDCLRFV VYQTGKGFCH LDTLHCFGQA
310 320 330 340 350 360
SGLCQLEKTL IDRKNNAPEG SYTARLFSDP KLLRAKIMEE AEELCDATTK ENVIWEMADL
370 380 390 400 410
MYFAITRCVG SGVSLNDISR HLDLKHRKVT RRKGDAKVAW QEKLKDKGGV ANTSYTA