GSHAB_PASMU
ID GSHAB_PASMU Reviewed; 757 AA.
AC Q9CM00;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutathione biosynthesis bifunctional protein GshAB {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GCS-GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00782};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE Includes:
DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GS {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00782};
DE Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00782};
DE AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00782};
GN Name=gshAB {ECO:0000255|HAMAP-Rule:MF_00782};
GN Synonyms=gshF {ECO:0000255|HAMAP-Rule:MF_00782}; OrderedLocusNames=PM1048;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: Synthesizes glutathione from L-glutamate and L-cysteine via
CC gamma-L-glutamyl-L-cysteine. {ECO:0000255|HAMAP-Rule:MF_00782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00782};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00782};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00782}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC cysteine ligase type 1 family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00782}.
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DR EMBL; AE004439; AAK03132.1; -; Genomic_DNA.
DR RefSeq; WP_010906990.1; NC_002663.1.
DR PDB; 3LN7; X-ray; 3.20 A; A/B=1-757.
DR PDBsum; 3LN7; -.
DR AlphaFoldDB; Q9CM00; -.
DR SMR; Q9CM00; -.
DR STRING; 747.DR93_920; -.
DR EnsemblBacteria; AAK03132; AAK03132; PM1048.
DR KEGG; pmu:PM1048; -.
DR PATRIC; fig|272843.6.peg.1062; -.
DR HOGENOM; CLU_020728_1_0_6; -.
DR OMA; EANFNPM; -.
DR SABIO-RK; Q9CM00; -.
DR UniPathway; UPA00142; UER00209.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00782; Glut_biosynth; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006335; Glut_biosynth.
DR InterPro; IPR006334; Glut_cys_ligase.
DR InterPro; IPR040657; GshAB_ATP-grasp.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR Pfam; PF18419; ATP-grasp_6; 1.
DR Pfam; PF04262; Glu_cys_ligase; 2.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01435; glu_cys_lig_rel; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutathione biosynthesis; Ligase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..757
FT /note="Glutathione biosynthesis bifunctional protein GshAB"
FT /id="PRO_0000192557"
FT DOMAIN 494..753
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT REGION 1..337
FT /note="Glutamate--cysteine ligase"
FT BINDING 521..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 702
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 723
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 723
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 725
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT BINDING 725
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00782"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 167..192
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 448..453
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 454..457
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 482..489
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 513..518
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 551..564
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 576..584
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 587..594
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 607..615
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 623..629
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 635..644
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 681..694
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 697..706
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:3LN7"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 720..727
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 730..734
FT /evidence="ECO:0007829|PDB:3LN7"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:3LN7"
FT HELIX 745..752
FT /evidence="ECO:0007829|PDB:3LN7"
SQ SEQUENCE 757 AA; 85862 MW; CF0E49A661C14336 CRC64;
MKIQHIIHEN QLGLLFQQGS FGLEKESQRV TADGAIVTTP HPAVFGNRRY HPYIQTDFAE
SQLELITPPT KKLEDTFRWL SVIHEVVQRS LPEEEYIFPL SMPAGLPAEE QIRVAQLDNP
EDVAYREYLV KIYGKNKQMV SGIHYNFQLS PDLITRLFRL QNEYQSAVDF QNDLYLKMAK
NFLRYQWILL YLLAATPTVE SAYFKDGSPL AKGQFVRSLR SSQYGYVNDP EINVSFDSVE
KYVESLEHWV STGKLIAEKE FYSNVRLRGA KKAREFLTTG IQYLEFRLFD LNPFEIYGIS
LKDAKFIHVF ALFMIWMDHT ADQEEVELGK ARLAEVAFEH PLEKTAYAVE GELVLLELLS
MLEQIGAEPE LFEIVKEKLT QFTDPSKTVA GRLVRAIEQA GSDQQLGAQL AQQYKAQAFE
RFYALSAFDN MELSTQALLF DVIQKGIHTE ILDENDQFLC LKYGDHIEYV KNGNMTSHDS
YISPLIMENK VVTKKVLQKA GFNVPQSVEF TSLEKAVASY ALFENRAVVI KPKSTNYGLG
ITIFQQGVQN REDFAKALEI AFREDKEVMV EDYLVGTEYR FFVLGDETLA VLLRVPANVV
GDSVHSVAEL VAMKNDHPLR GDGSRTPLKK IALGEIEQLQ LKEQGLTIDS IPAKDQLVQL
RANSNISTGG DSIDMTDEMH ESYKQLAVGI TKAMGAAVCG VDLIIPDLKQ PATPNLTSWG
VIEANFNPMM MMHIFPYAGK SRRLTQNVIK MLFPELE
