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UniProtKB - P50384 (TRPD_SACS2)

>sp|P50384|TRPD_SACS2 Anthranilate phosphoribosyltransferase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=trpD PE=1 SV=1
MNINEILKKLINKSDLEINEAEELAKAIIRGEVPEILVSAILVALRMKGESKNEIVGFAR
AMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSLVNPVAKHGNRAVSGKSGSAD
VLEALGYNIIVPPERAKELVNKTNFVFLFAQYYHPAMKNVANVRKTLGIRTIFNILGPLT
NPANAKYQLMGVFSKDHLDLLSKSAYELDFNKIILVYGEPGIDEVSPIGNTFMKIVSKRG
IEEVKLNVTDFGISPIPIEKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALD
RVGDFREGYEYADHLIEKSLDKLNEIISMNGDVTKLKTIVVKSSG

Entry version 147 (23 Feb 2022)
Sequence version 1 (01 Oct 1996)
Previous versions | rss

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Protein

Anthranilate phosphoribosyltransferase

Gene

trpD

Organism

Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).

UniRule annotation2 Publications

Catalytic activityⁱ

diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N-(5-phospho-β-D-ribosyl)anthranilate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
5-phospho-α-D-ribose 1-diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
anthranilate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00211
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus."
  Ivens A., Mayans O., Szadkowski H., Wilmanns M., Kirschner K.
  Eur. J. Biochem. 268:2246-2252(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CRYSTALLIZATION, SUBUNIT.
EC:
2.4.2.18
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00211
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus."
  Ivens A., Mayans O., Szadkowski H., Wilmanns M., Kirschner K.
  Eur. J. Biochem. 268:2246-2252(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CRYSTALLIZATION, SUBUNIT.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
diphosphate
zoom
+
N-(5-phospho-β-D-ribosyl)anthranilate
zoom
=
5-phospho-α-D-ribose 1-diphosphate
zoom
+
anthranilate
zoom

Cofactorⁱ

Mg²⁺Note: Binds 2 magnesium ions per monomer.

Kineticsⁱ

Pathwayⁱ: L-tryptophan biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	79	Anthranilate 1; via carbonyl oxygen	1
Binding siteⁱ	87	PhosphoribosylpyrophosphateUniRule annotation2 Publications	1
Metal bindingⁱ	91	Magnesium 1	1
Binding siteⁱ	109	Anthranilate 1	1
Binding siteⁱ	118	Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation2 Publications	1
Binding siteⁱ	164	Anthranilate 2	1
Metal bindingⁱ	223	Magnesium 2	1
Metal bindingⁱ	224	Magnesium 1	1
Metal bindingⁱ	224	Magnesium 2	1

GO - Molecular functionⁱ

anthranilate phosphoribosyltransferase activity Source: UniProtKB-UniRule
magnesium ion binding Source: UniProtKB-UniRule

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

tryptophan biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase
Biological process	Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	2.4.2.18, 6163
SABIO-RKⁱ	P50384
UniPathwayⁱ	UPA00035;UER00041

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Anthranilate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.18UniRule annotation)
Gene namesⁱ	Name:trpDUniRule annotation Ordered Locus Names:SSO0890
Organismⁱ	Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Taxonomic identifierⁱ	273057 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Archaea › TACK group › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Saccharolobus › Saccharolobus solfataricus
Proteomesⁱ	UP000001974 Componentⁱ: Chromosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	106	K → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency dedreases only 10-fold. 1 Publication	1
Mutagenesisⁱ	107	H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-178. 1 Publication	1
Mutagenesisⁱ	154	H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	164	R → A: Strong decrease of the affinity for anthranilate, although only a moderate 7-fold decrease in catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	178	P → A: 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-107.	1
Mutagenesisⁱ	223	D → N: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication	1
Mutagenesisⁱ	224	E → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000154523	1 – 345	Anthranilate phosphoribosyltransferaseAdd BLAST		345

Interactionⁱ

Subunit structureⁱ

Homodimer.

UniRule annotation4 Publications

Protein-protein interaction databases

STRINGⁱ	273057.SSO0890

STRINGⁱ

273057.SSO0890

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 11	Combined sources	9
Helixⁱ	18 – 29	Combined sources	12
Helixⁱ	35 – 48	Combined sources	14
Helixⁱ	52 – 65	Combined sources	14
Beta strandⁱ	75 – 79	Combined sources	5
Helixⁱ	90 – 98	Combined sources	9
Turnⁱ	99 – 101	Combined sources	3
Beta strandⁱ	104 – 108	Combined sources	5
Beta strandⁱ	112 – 115	Combined sources	4
Helixⁱ	118 – 125	Combined sources	8
Helixⁱ	133 – 143	Combined sources	11
Beta strandⁱ	144 – 149	Combined sources	6
Helixⁱ	150 – 153	Combined sources	4
Helixⁱ	155 – 159	Combined sources	5
Helixⁱ	161 – 167	Combined sources	7
Helixⁱ	172 – 175	Combined sources	4
Helixⁱ	177 – 179	Combined sources	3
Beta strandⁱ	186 – 191	Combined sources	6
Helixⁱ	195 – 205	Combined sources	11
Turnⁱ	207 – 209	Combined sources	3
Beta strandⁱ	211 – 218	Combined sources	8
Turnⁱ	219 – 221	Combined sources	3
Beta strandⁱ	222 – 224	Combined sources	3
Beta strandⁱ	227 – 237	Combined sources	11
Beta strandⁱ	240 – 247	Combined sources	8
Helixⁱ	248 – 251	Combined sources	4
Helixⁱ	258 – 260	Combined sources	3
Helixⁱ	266 – 277	Combined sources	12
Helixⁱ	282 – 298	Combined sources	17
Beta strandⁱ	301 – 304	Combined sources	4
Helixⁱ	305 – 316	Combined sources	12
Helixⁱ	319 – 329	Combined sources	11
Helixⁱ	333 – 340	Combined sources	8

Show more details

3D structure databases

SMRⁱ	P50384
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P50384

EvolutionaryTraceⁱ

P50384

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	77 – 79	Phosphoribosylpyrophosphate binding	3
Regionⁱ	82 – 83	Phosphoribosylpyrophosphate binding	2
Regionⁱ	89 – 92	Phosphoribosylpyrophosphate binding	4
Regionⁱ	106 – 114	Phosphoribosylpyrophosphate binding	9

Sequence similaritiesⁱ

Belongs to the anthranilate phosphoribosyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	arCOG02012, Archaea
HOGENOMⁱ	CLU_034315_2_1_2
InParanoidⁱ	P50384
OMAⁱ	LYHQSFK
PhylomeDBⁱ	P50384

Family and domain databases

Gene3Dⁱ	3.40.1030.10, 1 hit
HAMAPⁱ	MF_00211, TrpD, 1 hit
InterProⁱ	View protein in InterPro IPR005940, Anthranilate_Pribosyl_Tfrase IPR000312, Glycosyl_Trfase_fam3 IPR017459, Glycosyl_Trfase_fam3_N_dom IPR036320, Glycosyl_Trfase_fam3_N_dom)sf IPR035902, Nuc_phospho_transferase
PANTHERⁱ	PTHR43285, PTHR43285, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02885, Glycos_trans_3N, 1 hit PF00591, Glycos_transf_3, 1 hit
SUPFAMⁱ	SSF47648, SSF47648, 1 hit SSF52418, SSF52418, 1 hit
TIGRFAMsⁱ	TIGR01245, trpD, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P50384-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MNINEILKKL INKSDLEINE AEELAKAIIR GEVPEILVSA ILVALRMKGE 
        60         70         80         90        100
SKNEIVGFAR AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL 
       110        120        130        140        150
VNPVAKHGNR AVSGKSGSAD VLEALGYNII VPPERAKELV NKTNFVFLFA 
       160        170        180        190        200
QYYHPAMKNV ANVRKTLGIR TIFNILGPLT NPANAKYQLM GVFSKDHLDL 
       210        220        230        240        250
LSKSAYELDF NKIILVYGEP GIDEVSPIGN TFMKIVSKRG IEEVKLNVTD 
       260        270        280        290        300
FGISPIPIEK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD 
       310        320        330        340 
RVGDFREGYE YADHLIEKSL DKLNEIISMN GDVTKLKTIV VKSSG

Length:345

Mass (Da):37,574

Last modified:October 1, 1996 - v1

Checksum:ⁱD51927F4B7AAFA90

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Z50014 Genomic DNA Translation: CAA90309.1 AE006641 Genomic DNA Translation: AAK41173.1
PIRⁱ	F90239
NCBI Reference Sequences More...RefSeqⁱ	WP_009992305.1, NC_002754.1

Genome annotation databases

EnsemblBacteriaⁱ	AAK41173; AAK41173; SSO0890
GeneIDⁱ	44129821
KEGGⁱ	sso:SSO0890
PATRICⁱ	fig\|273057.12.peg.894

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P50384	Anthranilate phosphoribosyltransferase		SACSO		345	UniRef100_P50384
Anthranilate phosphoribosyltransferase		SACS9		345

Protein	Similar proteins		Species	Score	Length	Source
P50384	Anthranilate phosphoribosyltransferase		SULIK		345	UniRef90_P50384
Anthranilate phosphoribosyltransferase		SULIM		345
Anthranilate phosphoribosyltransferase		SULIN		345
Anthranilate phosphoribosyltransferase		SULIA		345
Anthranilate phosphoribosyltransferase		SULIL		345
+13

Protein	Similar proteins		Species	Score	Length	Source
P50384	Anthranilate phosphoribosyltransferase		SULIA		345	UniRef50_P50384
Anthranilate phosphoribosyltransferase		SULIN		345
Anthranilate phosphoribosyltransferase		SULIL		345
Anthranilate phosphoribosyltransferase		SULIY		345
Anthranilate phosphoribosyltransferase		SULIK		345
+47

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Z50014 Genomic DNA Translation: CAA90309.1 AE006641 Genomic DNA Translation: AAK41173.1
PIRⁱ	F90239
RefSeqⁱ	WP_009992305.1, NC_002754.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GXB	X-ray	2.70	A/B/C/D	1-345	[»]
	1O17	X-ray	2.05	A/B/C/D	1-345	[»]
	1ZXY	X-ray	2.56	A/B/C/D	1-345	[»]
	1ZYK	X-ray	2.40	A/B/C/D	1-345	[»]
	2GVQ	X-ray	2.43	A/B/C/D	1-345	[»]
	3GBR	X-ray	2.25	A/B	1-345	[»]
SMRⁱ	P50384
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	273057.SSO0890

STRINGⁱ

273057.SSO0890

Genome annotation databases

EnsemblBacteriaⁱ	AAK41173; AAK41173; SSO0890
GeneIDⁱ	44129821
KEGGⁱ	sso:SSO0890
PATRICⁱ	fig\|273057.12.peg.894

Phylogenomic databases

eggNOGⁱ	arCOG02012, Archaea
HOGENOMⁱ	CLU_034315_2_1_2
InParanoidⁱ	P50384
OMAⁱ	LYHQSFK
PhylomeDBⁱ	P50384

Enzyme and pathway databases

UniPathwayⁱ	UPA00035;UER00041
BRENDAⁱ	2.4.2.18, 6163
SABIO-RKⁱ	P50384

Miscellaneous databases

EvolutionaryTraceⁱ	P50384

EvolutionaryTraceⁱ

P50384

Family and domain databases

Gene3Dⁱ	3.40.1030.10, 1 hit
HAMAPⁱ	MF_00211, TrpD, 1 hit
InterProⁱ	View protein in InterPro IPR005940, Anthranilate_Pribosyl_Tfrase IPR000312, Glycosyl_Trfase_fam3 IPR017459, Glycosyl_Trfase_fam3_N_dom IPR036320, Glycosyl_Trfase_fam3_N_dom)sf IPR035902, Nuc_phospho_transferase
PANTHERⁱ	PTHR43285, PTHR43285, 1 hit
Pfamⁱ	View protein in Pfam PF02885, Glycos_trans_3N, 1 hit PF00591, Glycos_transf_3, 1 hit
SUPFAMⁱ	SSF47648, SSF47648, 1 hit SSF52418, SSF52418, 1 hit
TIGRFAMsⁱ	TIGR01245, trpD, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TRPD_SACS2
Accessionⁱ	P50384Primary (citable) accession number: P50384
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
	Last sequence update:	October 1, 1996
	Last modified:	February 23, 2022
	This is version 147 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniParc

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Annotation systems

Supporting data

UniProtKB - P50384 (TRPD_SACS2)

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Anthranilate phosphoribosyltransferase

trpD

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-tryptophan biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: L-tryptophan biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ