GCS2_MICLC
ID GCS2_MICLC Reviewed; 398 AA.
AC C5CC09;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN OrderedLocusNames=Mlut_16620;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000255|HAMAP-Rule:MF_01609}.
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_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR EMBL; CP001628; ACS31150.1; -; Genomic_DNA.
DR RefSeq; WP_012751033.1; NZ_LS483396.1.
DR AlphaFoldDB; C5CC09; -.
DR SMR; C5CC09; -.
DR STRING; 465515.Mlut_16620; -.
DR PRIDE; C5CC09; -.
DR EnsemblBacteria; ACS31150; ACS31150; Mlut_16620.
DR KEGG; mlu:Mlut_16620; -.
DR PATRIC; fig|465515.4.peg.1600; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_0_11; -.
DR OMA; LIFGLHV; -.
DR OrthoDB; 991285at2; -.
DR Proteomes; UP000000738; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..398
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_1000215703"
SQ SEQUENCE 398 AA; 42931 MW; 43BC21EC2B88ECBA CRC64;
MTLPFADSAQ STLGIEWELA LVDAVSGELR SEAPDLLRAL HVAEGLADDD VNPHMTSELL
QNTVELVTGV HERVDAATAD LGRIAARVAD AAAARGISLF CQGTHPFADA IAQPSTPSER
YDRMLDLTQY WGRQLLIFGV HVHVGLDDVS KAMPVVNGLV NRVPHLLALS ASSPFWAGTD
TGYQSQRTLL FQQLPTAGLP FQFQEWEDFE RCVAQMEQVG MIADVTECRW DVRAVPRLGT
VEMRACDGLA TLEEIAAVTA YTQCLVDDLS ASLERGETVE VLPPWHAQEN KWRAARYGMD
ATVIVDARGT QVPLAEHLPA EIERLTPVAE RLGCEAELAG VQAMIDDGGA ARQRRVEAQA
LAGPPAEGED ADDAVAPLRA VVLDAAARTR ASLDGRTG
