P60759 (HIS1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP phosphoribosyltransferase
Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17

Gene names

Name:	hisG
Ordered Locus Names:	Rv2121c, MT2181
ORF Names:	MTCY261.17c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. HAMAP MF_00079
Catalytic activity	1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079
Cofactor	Magnesium.
Enzyme regulation	Feedback inhibited by histidine. Also inhibited by AMP. HAMAP MF_00079
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00079
Subunit structure	Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme.
Subcellular location	Cytoplasm By similarity HAMAP MF_00079.
Sequence similarities	Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE histidine biosynthetic process Inferred from direct assay Ref.3. Source: MTBBASE protein homooligomerization Inferred from physical interaction Ref.3. Source: MTBBASE
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	AMP binding Inferred from direct assay Ref.3. Source: MTBBASE ATP binding Inferred from direct assay Ref.3. Source: MTBBASE ATP phosphoribosyltransferase activity Inferred from direct assay Ref.3. Source: MTBBASE magnesium ion binding Inferred from direct assay Ref.3. Source: MTBBASE protein homodimerization activity Inferred from physical interaction Ref.3. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 284

284

ATP phosphoribosyltransferase HAMAP MF_00079

PRO_0000151857

Secondary structure

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284

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Helix

13 – 22

10

Beta strand

34 – 38

5

Turn

39 – 42

4

Beta strand

43 – 48

6

Helix

50 – 52

3

Helix

53 – 59

7

Beta strand

63 – 68

6

Helix

69 – 75

7

Beta strand

79 – 84

6

Beta strand

90 – 97

8

Helix

104 – 107

4

Beta strand

111 – 115

5

Helix

117 – 127

11

Beta strand

132 – 135

4

Helix

142 – 145

4

Beta strand

150 – 159

10

Helix

160 – 164

5

Beta strand

167 – 177

11

Beta strand

179 – 184

6

Helix

195 – 209

15

Beta strand

212 – 220

9

Helix

221 – 223

3

Helix

224 – 230

7

Beta strand

234 – 236

3

Beta strand

238 – 241

4

Beta strand

247 – 255

9

Helix

256 – 258

3

Helix

259 – 268

10

Beta strand

272 – 277

6

Sequences

	Sequence		Length	Mass (Da)
	P60759 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: C248C57399302B2A	FASTA	284	30,481
	10 20 30 40 50 60 MLRVAVPNKG ALSEPATEIL AEAGYRRRTD SKDLTVIDPV NNVEFFFLRP KDIAIYVGSG 70 80 90 100 110 120 ELDFGITGRD LVCDSGAQVR ERLALGFGSS SFRYAAPAGR NWTTADLAGM RIATAYPNLV 130 140 150 160 170 180 RKDLATKGIE ATVIRLDGAV EISVQLGVAD AIADVVGSGR TLSQHDLVAF GEPLCDSEAV 190 200 210 220 230 240 LIERAGTDGQ DQTEARDQLV ARVQGVVFGQ QYLMLDYDCP RSALKKATAI TPGLESPTIA 250 260 270 280 PLADPDWVAI RALVPRRDVN GIMDELAAIG AKAILASDIR FCRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis." Cho Y., Sharma V., Sacchettini J.C. J. Biol. Chem. 278:8333-8339(2003) [PubMed: 12511575] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH HISTIDINE AND AMP. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842578 Genomic DNA. Translation: CAB10710.1.
AE000516 Genomic DNA. Translation: AAK46464.1.

PIR

D70513.

RefSeq

NP_216637.1. NC_000962.2.
NP_336650.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NH7	X-ray	2.70	A	1-284	[»]
1NH8	X-ray	1.80	A	1-284	[»]

ProteinModelPortal

P60759.

SMR

P60759. Positions 1-284.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003475; EBMYCP00000003475; EBMYCG00000003473.
EBMYCT00000071384; EBMYCP00000069443; EBMYCG00000071379.

GeneID

888689.
924287.

GenomeReviews

Gene locus MT2181 in contig AE000516_GR.
Gene locus Rv2121c in contig AL123456_GR.

KEGG

mtc:MT2181.
mtu:Rv2121c.

PATRIC

18126552. VBIMycTub22151_2389.

TIGR

MT2181.

Organism-specific databases

TubercuList

Rv2121c.

Phylogenomic databases

GeneTree

EBGT00050000017405.

HOGENOM

HBG391868.

OMA

IMLHAPS.

PhylomeDB

P60759.

ProtClustDB

PRK00489.

Family and domain databases

HAMAP

MF_00079. HisG_Long.
[Tree]

InterPro

IPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]

Gene3D

G3DSA:3.30.70.120. PII_glnB. 1 hit.

KO

K00765.

PANTHER

PTHR21403. ATP_phspho_trans. 1 hit.

Pfam

PF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]

SUPFAM

SSF54913. N-reg_PII-like_a/b. 1 hit.

TIGRFAMs

TIGR00070. HisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.

PROSITE

PS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

HIS1_MYCTU

Accession

Primary (citable) accession number: P60759
Secondary accession number(s): O33256

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program