Reviewed, UniProtKB/Swiss-Prot P37528 (PDXT_BACSU)

Names and origin

Protein names

Recommended name:
    Glutamine amidotransferase subunit pdxT
    EC=2.6.-.-
Alternative name(s):
    Glutamine amidotransferase glutaminase subunit pdxT

Gene names

Name:	pdxT
Synonyms:	yaaE
Ordered Locus Names:	BSU00120

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the hydrolysis of glutamine to glutamate and ammonia. Channels an ammonia molecule to pdxS. HAMAP MF_01615
Pathway	Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. HAMAP MF_01615
Subunit structure	Forms a complex with pdxS. HAMAP MF_01615
Miscellaneous	The pathway is different from the classical pdxA-pdxJ pathway. HAMAP MF_01615
Sequence similarities	Belongs to the glutamine amidotransferase pdxT/SNO family.

Ontologies

Keywords
Domain	Glutamine amidotransferase
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glutamine catabolic process Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	transferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

Glutamine amidotransferase subunit pdxT HAMAP MF_01615

PRO_0000135632

Sites

Active site

79

1

Nucleophile HAMAP MF_01615

Active site

170

1

HAMAP MF_01615

Active site

172

1

HAMAP MF_01615

Binding site

106

1

Glutamine Potential

Secondary structure

1

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196

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Beta strand

9 – 11

3

Helix

14 – 22

9

Beta strand

26 – 30

5

Helix

33 – 38

6

Beta strand

40 – 44

5

Helix

49 – 58

10

Helix

62 – 70

9

Beta strand

75 – 78

4

Helix

80 – 85

6

Beta strand

102 – 105

4

Turn

111 – 113

3

Beta strand

114 – 120

7

Beta strand

129 – 135

7

Beta strand

138 – 142

5

Beta strand

147 – 152

6

Beta strand

155 – 161

7

Beta strand

164 – 169

6

Beta strand

173 – 175

3

Helix

178 – 193

16

Sequences

	Sequence		Length	Mass (Da)
	P37528-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 91111DEF75257882	FASTA	196	21,447
	10 20 30 40 50 60 MLTIGVLGLQ GAVREHIHAI EACGAAGLVV KRPEQLNEVD GLILPGGEST TMRRLIDTYQ 70 80 90 100 110 120 FMEPLREFAA QGKPMFGTCA GLIILAKEIA GSDNPHLGLL NVVVERNSFG RQVDSFEADL 130 140 150 160 170 180 TIKGLDEPFT GVFIRAPHIL EAGENVEVLS EHNGRIVAAK QGQFLGCSFH PELTEDHRVT 190 QLFVEMVEEY KQKALV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis." Belitsky B.R. J. Bacteriol. 186:1191-1196(2004) [PubMed: 14762015] [Abstract] Cited for: CHARACTERIZATION. Strain: 168 / SMY.
[4]	"Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis." Bauer J.A., Bennett E.M., Begley T.P., Ealick S.E. J. Biol. Chem. 279:2704-2711(2004) [PubMed: 14585832] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D26185 Genomic DNA. Translation: BAA05248.1.
AL009126 Genomic DNA. Translation: CAB11788.1.

PIR

S66042.

RefSeq

NP_387893.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R9G	X-ray	2.50	A/B	1-196	[»]
2NV0	X-ray	1.73	A/B	1-196	[»]
2NV2	X-ray	2.12	B/D/F/H/J/L/N/P/R/T/V/X	1-196	[»]

ModBase

Search...

Genome annotation databases

GeneID

939971.

GenomeReviews

Gene locus BSU00120 in contig AL009126_GR.

KEGG

bsu:BSU00120.

NMPDR

fig|224308.1.peg.12.

Organism-specific databases

SubtiList

BG10076. pdxT. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P37528.

OMA

QGDVREH

Family and domain databases

HAMAP

MF_01615.
[Tree]

InterPro

IPR002161. SNO.
[Graphical view]

Pfam

PF01174. SNO. 1 hit.
[Graphical view]

PIRSF

PIRSF005639. Glut_amidoT_SNO. 1 hit.

PROSITE

PS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PDXT_BACSU

Accession

Primary (citable) accession number: P37528

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 24, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)