Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.UniRule annotation

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Pathwayi: glutathione biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
  2. Glutathione biosynthesis bifunctional protein GshAB (gshAB)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi702Magnesium or manganese 1UniRule annotation1
Metal bindingi723Magnesium or manganese 1UniRule annotation1
Metal bindingi723Magnesium or manganese 2UniRule annotation1
Metal bindingi725Magnesium or manganese 2UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi521 – 580ATPUniRule annotationAdd BLAST60

GO - Molecular functioni

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ9CM00.
UniPathwayiUPA00142; UER00209.
UPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione biosynthesis bifunctional protein GshABUniRule annotation
Alternative name(s):
Gamma-GCS-GSUniRule annotation
Short name:
GCS-GSUniRule annotation
Including the following 2 domains:
Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
Alternative name(s):
Gamma-ECSUniRule annotation
Short name:
GCSUniRule annotation
Gamma-glutamylcysteine synthetaseUniRule annotation
Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
Alternative name(s):
GSH synthetaseUniRule annotation
Short name:
GSUniRule annotation
Short name:
GSH-SUniRule annotation
Short name:
GSHaseUniRule annotation
Glutathione synthaseUniRule annotation
Gene namesi
Name:gshABUniRule annotation
Synonyms:gshFUniRule annotation
Ordered Locus Names:PM1048
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
Proteomesi
  • UP000000809 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001925571 – 757Glutathione biosynthesis bifunctional protein GshABAdd BLAST757

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi272843.PM1048.

Structurei

Secondary structure

1757
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 10Combined sources6
Helixi13 – 17Combined sources5
Beta strandi19 – 28Combined sources10
Beta strandi34 – 36Combined sources3
Beta strandi43 – 45Combined sources3
Turni48 – 50Combined sources3
Beta strandi52 – 55Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi62 – 72Combined sources11
Helixi73 – 90Combined sources18
Beta strandi100 – 102Combined sources3
Turni109 – 111Combined sources3
Helixi120 – 133Combined sources14
Helixi136 – 139Combined sources4
Beta strandi144 – 149Combined sources6
Helixi151 – 160Combined sources10
Turni162 – 164Combined sources3
Helixi167 – 192Combined sources26
Turni204 – 206Combined sources3
Beta strandi217 – 219Combined sources3
Beta strandi222 – 225Combined sources4
Helixi239 – 251Combined sources13
Beta strandi256 – 258Combined sources3
Beta strandi264 – 269Combined sources6
Helixi273 – 275Combined sources3
Helixi276 – 279Combined sources4
Beta strandi283 – 286Combined sources4
Helixi301 – 316Combined sources16
Helixi323 – 338Combined sources16
Helixi348 – 364Combined sources17
Helixi369 – 383Combined sources15
Helixi385 – 387Combined sources3
Helixi389 – 399Combined sources11
Beta strandi400 – 402Combined sources3
Helixi403 – 419Combined sources17
Turni420 – 423Combined sources4
Turni427 – 430Combined sources4
Helixi433 – 445Combined sources13
Beta strandi448 – 453Combined sources6
Turni454 – 457Combined sources4
Beta strandi458 – 463Combined sources6
Beta strandi466 – 471Combined sources6
Turni472 – 474Combined sources3
Beta strandi477 – 481Combined sources5
Helixi482 – 489Combined sources8
Helixi491 – 500Combined sources10
Beta strandi507 – 511Combined sources5
Helixi513 – 518Combined sources6
Helixi519 – 522Combined sources4
Beta strandi523 – 526Combined sources4
Beta strandi528 – 534Combined sources7
Turni537 – 540Combined sources4
Helixi551 – 564Combined sources14
Beta strandi566 – 572Combined sources7
Beta strandi576 – 584Combined sources9
Beta strandi587 – 594Combined sources8
Beta strandi597 – 600Combined sources4
Helixi601 – 603Combined sources3
Helixi607 – 615Combined sources9
Beta strandi623 – 629Combined sources7
Helixi635 – 644Combined sources10
Beta strandi648 – 650Combined sources3
Beta strandi657 – 659Combined sources3
Helixi666 – 668Combined sources3
Beta strandi672 – 674Combined sources3
Turni676 – 678Combined sources3
Helixi681 – 694Combined sources14
Beta strandi697 – 706Combined sources10
Beta strandi708 – 710Combined sources3
Turni716 – 718Combined sources3
Beta strandi720 – 727Combined sources8
Helixi730 – 734Combined sources5
Beta strandi737 – 739Combined sources3
Helixi745 – 752Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LN7X-ray3.20A/B1-757[»]
ProteinModelPortaliQ9CM00.
SMRiQ9CM00.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini494 – 753ATP-graspUniRule annotationAdd BLAST260

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 337Glutamate--cysteine ligaseAdd BLAST337

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D9M. Bacteria.
COG1181. LUCA.
COG2918. LUCA.
HOGENOMiHOG000156471.
KOiK01919.
OMAiEANFNPM.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPiMF_00782. Glut_biosynth. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR003806. ATP-grasp_DUF201-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view]
PfamiPF02655. ATP-grasp_3. 1 hit.
PF04262. Glu_cys_ligase. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CM00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIQHIIHEN QLGLLFQQGS FGLEKESQRV TADGAIVTTP HPAVFGNRRY
60 70 80 90 100
HPYIQTDFAE SQLELITPPT KKLEDTFRWL SVIHEVVQRS LPEEEYIFPL
110 120 130 140 150
SMPAGLPAEE QIRVAQLDNP EDVAYREYLV KIYGKNKQMV SGIHYNFQLS
160 170 180 190 200
PDLITRLFRL QNEYQSAVDF QNDLYLKMAK NFLRYQWILL YLLAATPTVE
210 220 230 240 250
SAYFKDGSPL AKGQFVRSLR SSQYGYVNDP EINVSFDSVE KYVESLEHWV
260 270 280 290 300
STGKLIAEKE FYSNVRLRGA KKAREFLTTG IQYLEFRLFD LNPFEIYGIS
310 320 330 340 350
LKDAKFIHVF ALFMIWMDHT ADQEEVELGK ARLAEVAFEH PLEKTAYAVE
360 370 380 390 400
GELVLLELLS MLEQIGAEPE LFEIVKEKLT QFTDPSKTVA GRLVRAIEQA
410 420 430 440 450
GSDQQLGAQL AQQYKAQAFE RFYALSAFDN MELSTQALLF DVIQKGIHTE
460 470 480 490 500
ILDENDQFLC LKYGDHIEYV KNGNMTSHDS YISPLIMENK VVTKKVLQKA
510 520 530 540 550
GFNVPQSVEF TSLEKAVASY ALFENRAVVI KPKSTNYGLG ITIFQQGVQN
560 570 580 590 600
REDFAKALEI AFREDKEVMV EDYLVGTEYR FFVLGDETLA VLLRVPANVV
610 620 630 640 650
GDSVHSVAEL VAMKNDHPLR GDGSRTPLKK IALGEIEQLQ LKEQGLTIDS
660 670 680 690 700
IPAKDQLVQL RANSNISTGG DSIDMTDEMH ESYKQLAVGI TKAMGAAVCG
710 720 730 740 750
VDLIIPDLKQ PATPNLTSWG VIEANFNPMM MMHIFPYAGK SRRLTQNVIK

MLFPELE
Length:757
Mass (Da):85,862
Last modified:June 1, 2001 - v1
Checksum:iCF0E49A661C14336
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK03132.1.
RefSeqiWP_010906990.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK03132; AAK03132; PM1048.
GeneIDi1244395.
KEGGipmu:PM1048.
PATRICi22871339. VBIPasMul88067_1062.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK03132.1.
RefSeqiWP_010906990.1. NC_002663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LN7X-ray3.20A/B1-757[»]
ProteinModelPortaliQ9CM00.
SMRiQ9CM00.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272843.PM1048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK03132; AAK03132; PM1048.
GeneIDi1244395.
KEGGipmu:PM1048.
PATRICi22871339. VBIPasMul88067_1062.

Phylogenomic databases

eggNOGiENOG4105D9M. Bacteria.
COG1181. LUCA.
COG2918. LUCA.
HOGENOMiHOG000156471.
KOiK01919.
OMAiEANFNPM.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00209.
UPA00142; UER00210.
SABIO-RKQ9CM00.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPiMF_00782. Glut_biosynth. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR003806. ATP-grasp_DUF201-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view]
PfamiPF02655. ATP-grasp_3. 1 hit.
PF04262. Glu_cys_ligase. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHAB_PASMU
AccessioniPrimary (citable) accession number: Q9CM00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.