STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
hisFImidazole glycerol phosphate synthase subunit hisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. (262 aa)    
Predicted Functional Partners:
hisA
PMID: 2664449 best DB hits: BLAST: swissprot:P74561; HIS4_SYNY3; E=3e-56 pir:A83003; phosphoribosylformimino-5-aminoimidazole carboxamide; E=5e-49 gb:AAF05093.1; AF150930_2 (AF150930) phosphoribosyl; E=2e-46 COG: slr0652; COG0106 Phosphoribosylformimino-5-aminoimidazole; E=3e-57 PA5141; COG0106 Phosphoribosylformimino-5-aminoimidazole carboxamide; E=5e-50 NMB0629; COG0106 Phosphoribosylformimino-5-aminoimidazole; E=6e-44 PFAM: PF00977; Histidine biosynthesis protein; E=4.7e-70.
 
0.999
hisH
Amidotransferase hisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
 0.999
hisI
phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
  
 0.998
hisBD
Best DB hits: BLAST: ddbj:BAB07300.1; (AP001519) imidazoleglycerol-phosphate; E=3e-49 swissprot:O33564; HIS7_RHOSH IMIDAZOLEGLYCEROL-PHOSPHATE; E=1e-48 swissprot:P34047; HIS7_ARATH IMIDAZOLEGLYCEROL-PHOSPHATE; E=2e-48 COG: BH3581; COG0131 Imidazoleglycerol-phosphate dehydratase; E=3e-50 PFAM: PF00475; Imidazoleglycerol-phosphate dehydrat; E=7e-96.
 
 0.998
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.993
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
 
  
 0.978
hisC
Histidinol-phosphate aminotransferase; PMID: 1400209 best DB hits: BLAST: swissprot:P73807; HIS8_SYNY3 HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; E=1e-56 swissprot:P45358; HIS8_ACEXY HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; E=2e-52 gb:AAK00147.1; AF222753_2 (AF222753) putative aminotransferase; E=2e-43 COG: sll1958; COG0079 Histidinol-phosphate aminotransferase/Tyrosine; E=1e-57 PFAM: PF00155; Aminotransferase class-I; E=5.1e-06 PF00222; Aminotransferase class-II; E=1.3e-17; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase s [...]
 
  
 0.974
hisI-2
Probable phosphoribosyl-ATP pyrophosphatase; PMID: 3062174 best DB hits: BLAST: swissprot:O30723; HIS2_RHOCA PHOSPHORIBOSYL-ATP PYROPHOSPHATASE; E=2e-10 swissprot:P26722; HIS2_AZOBR PHOSPHORIBOSYL-ATP PYROPHOSPHATASE; E=6e-08 pir:D81178; phosphoribosyl-ATP cyclohydrolase NMB0603 [imported] -; E=8e-08 COG: NMB0603; COG0140 Phosphoribosyl-ATP pyrophosphohydrolase; E=8e-09 PFAM: PF01503; Phosphoribosyl-ATP pyrophosphohydrol; E=9.2e-30.
 
  
 0.968
purH
Bifunctional purine biosynthesis protein purH; PMID: 3036807 best DB hits: BLAST: swissprot:P12048; PUR9_BACSU BIFUNCTIONAL PURINE BIOSYNTHESIS; E=1e-125 ddbj:BAB04352.1; (AP001509); E=1e-124 gb:AAF33520.1; (AF170176) Salmonella typhimurium; E=1e-118 COG: BS_purH; COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only; E=1e-126 purH; COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP; E=1e-119 HI0887; COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only; E=1e-118 PFAM: PF02142; MGS-like domain; E=2.2e-46 PF01808; AICARFT/IMPCHase bienzyme; E=1.3e-113.
  
 
 0.928
RB6292
Conserved hypothetical protein; PMID: 8688087 best DB hits: BLAST: swissprot:Q58114; Y703_METJA HYPOTHETICAL PROTEIN MJ0703 -----; E=9e-14 gb:AAG32955.1; (AF032114) unknown [Methylobacterium extorquens]; E=6e-07 pir:A69189; phosphoribosylformimino-5-aminoimidazole carboxamide; E=4e-05 COG: MJ0703; COG1411 Archaeal family of HisA paralogs; E=9e-15; Belongs to the HisA/HisF family.
     
 0.918
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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