ID A0A1B6ZAE6_9SPHN Unreviewed; 457 AA.
AC A0A1B6ZAE6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=A8B75_11890 {ECO:0000313|EMBL:OAO02629.1};
OS Sphingomonadales bacterium EhC05.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1849171 {ECO:0000313|EMBL:OAO02629.1, ECO:0000313|Proteomes:UP000078455};
RN [1] {ECO:0000313|Proteomes:UP000078455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC05 {ECO:0000313|Proteomes:UP000078455};
RA Rosana A., Orata F., Boucher Y., Case R.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC).
CC {ECO:0000256|PIRNR:PIRNR017901}.
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:0000256|PIRNR:PIRNR017901};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006}.
CC -!- SUBUNIT: Homodimer or monomer when oxidized or reduced, respectively.
CC {ECO:0000256|ARBA:ARBA00011153}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the carboxylate-amine ligase family.
CC Glutamate--cysteine ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010253}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC EgtA subfamily. {ECO:0000256|PIRNR:PIRNR017901}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAO02629.1}.
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DR EMBL; LXYP01000014; OAO02629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6ZAE6; -.
DR STRING; 1849171.A8B75_11890; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000078455; Unassembled WGS sequence.
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:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.590.20; -; 1.
DR InterPro; IPR035434; GCL_bact_plant.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011556; Glut_cys_lig_pln_type.
DR NCBIfam; TIGR01436; glu_cys_lig_pln; 1.
DR PANTHER; PTHR34378; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR34378:SF1; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR017901-50};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Ligase {ECO:0000256|PIRNR:PIRNR017901, ECO:0000313|EMBL:OAO02629.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000078455};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 114..334
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 457 AA; 50849 MW; 71633A772A9ECDC1 CRC64;
MSTRQVSNSN DPIIEDISQL IEPMQGGEKP KEQWRIGTEH EKFVYCTTDH HAPSYDEPGG
IKDLLLALQE FGWKPVEENG KVIAMAGDDG TVSLEPAGQL ELSGAPLENL HETCNETGRH
LQQVKAIGQK TGKGFLGLGM WPDKTRAELP IMPKGRYGIM LDHMPRVGEL GLDMMLRTCT
IQVNLDYSSE ADMAQKFRVG LALQPLATAL FANSPFTENK PNGYQSFRSH IWSDTDPHRT
GMLPFVFEDN FGYERYAQYM LDVPMYFVFR DGKYIDAAGL SFRDFLKGEL SVLPGEKPSI
SDWNDHLSTA FPEVRLKSFL EMRGADGGPW NRICALPAFW VGLLYDQTAL DAAWDRVKGW
TMEEREALRN AVPEQGLDAP IPNGGKLLDL AGEILEIASS GLTARGRLNT SGDNESGFLD
PLRDVVAKGK SPAAQLLDRY HGDWNGDVSK IYDELSF
//
