STRINGSTRING
hisD hisD hisS hisS hisZ hisZ hisG hisG hisI hisI hisD-2 hisD-2 hisE hisE hisF hisF hisA hisA hisH hisH hisB hisB
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.
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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
Your Input:
hisDHistidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (434 aa)
hisSTIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; KEGG: sme:SMc00919 probable histidyl-tRNA synthetase protein. (507 aa)
hisZtRNA synthetase class II (G H P and S); Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (377 aa)
hisGATP 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. Short subfamily. (231 aa)
hisIPhosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. (151 aa)
hisD-2Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (432 aa)
hisEPFAM: phosphoribosyl-ATP pyrophosphohydrolase; KEGG: sme:SMc02568 probable phosphoribosyl-ATP pyrophosphatase protein. (107 aa)
hisFImidazoleglycerol phosphate synthase, cyclase subunit; 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. (258 aa)
hisATIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; PFAM: histidine biosynthesis protein; KEGG: sme:SMc02570 probable phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase protein. (248 aa)
hisHImidazole glycerol phosphate synthase, glutamine amidotransferase subunit; 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. (216 aa)
hisBPFAM: imidazoleglycerol-phosphate dehydratase; KEGG: sme:SMc02574 probable imidazoleglycerol-phosphate dehydratase protein. (202 aa)
Your Current Organism:
Sinorhizobium medicae
NCBI taxonomy Id: 366394
Other names: Ensifer medicae WSM419, S. medicae WSM419, Sinorhizobium medicae WSM419
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