Cystathionine gamma-synthase - Nicotiana tabacum (Common tobacco)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Cystathionine gamma-synthase EMBL AAD16143.1

Gene names

Name:

metB EMBL AAD16143.1

Organism

Nicotiana tabacum (Common tobacco) EMBL AAD16143.1

Taxonomic identifier

4097 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Cofactor	Pyridoxal phosphate By similarity. RuleBase RU004507
Sequence similarities	Belongs to the trans-sulfuration enzymes family. RuleBase RU004079

Ontologies

Keywords
Ligand	Pyridoxal phosphate RuleBase RU004507
Technical term	3D-structure PDB 1I48 PDB 1I41 PDB 1QGN PDB 1I43
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Molecular_function	catalytic activity Inferred from electronic annotation. Source: InterPro pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Site

163

1

Important for catalytic activity PDB 1QGN

Site

236

1

Important for catalytic activity PDB 1QGN

Site

261

1

Important for catalytic activity PDB 1QGN

Amino acid modifications

Modified residue

261

1

N6-(pyridoxal phosphate)lysine PDB 1I48 PDB 1QGN PDB 1I43

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZPL5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D2936EDA41F02D44
Show »

FASTA

445

48,017

        10         20         30         40         50         60 
MAKAVDAAAA AAAAIAPVDT TVVNEDVALV ENETCNDQNV QFDSLPSMKY ASFLNSDGSV 

        70         80         90        100        110        120 
AIHAGERLGR GIVTDAITTP VVNTSAYFFN KTSELIDFKE KRRASFEYGR YGNPTTVVLE 

       130        140        150        160        170        180 
EKISALEGAE STLLMASGMC ASTVMLLALV PAGGHIVTTT DCYRKTRIFI ETILPKMGIT 

       190        200        210        220        230        240 
ATVIDPADVG ALELALNQKK VNLFFTESPT NPFLRCVDIE LVSKLCHEKG ALVCIDGTFA 

       250        260        270        280        290        300 
TPLNQKALAL GADLVLHSAT KFLGGHNDVL AGCISGPLKL VSEIRNLHHI LGGALNPNAA 

       310        320        330        340        350        360 
YLIIRGMKTL HLRVQQQNST ALRMAEILEA HPKVRHVYYP GLQSHPEHHI AKKQMTGFGG 

       370        380        390        400        410        420 
AVSFEVDGDL LTTAKFVDAL KIPYIAPSFG GCESIVDQPA IMSYWDLSQS DRAKYGIMDN 

       430        440 
LVRFSFGVED FDDLKADILQ ALDSI

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References

[1]	"Cloning, purification and characterization of cystathionine gamma-synthase from Nicotiana tabacum." Clausen T., Laber B., Streber W. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity." Steegborn C., Messerschmidt A., Laber B., Streber W., Huber R., Clausen T. J. Mol. Biol. 290:983-996(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), ACTIVE SITE, AND PYRIDOXAL PHOSPHATE AT LYS-261.
[3]	"Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor." Steegborn C., Laber B., Messerschmidt A., Huber R., Clausen T. J. Mol. Biol. 311:789-801(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-261.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF097180 mRNA. Translation: AAD16143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I41	X-ray	3.20	A/B/C/D/E/F/G/H/I/J/K/L	1-445	[»]
1I43	X-ray	3.10	A/B/C/D/E/F/G/H/I/J/K/L	1-445	[»]
1I48	X-ray	3.25	A/B/C/D/E/F/G/H/I/J/K/L	1-445	[»]
1QGN	X-ray	2.90	A/B/C/D/E/F/G/H	1-445	[»]

ProteinModelPortal

Q9ZPL5.

SMR

Q9ZPL5. Positions 49-445.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

PANTHER

PTHR11808. PTHR11808. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9ZPL5.

Entry information

Entry name

Q9ZPL5_TOBAC

Accession

Primary (citable) accession number: Q9ZPL5

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)