(data stored in ACNUC7421 zone)

SWISSPROT: E6S8N6_INTC7

ID   E6S8N6_INTC7            Unreviewed;       374 AA.
AC   E6S8N6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 45.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Intca_0457 {ECO:0000313|EMBL:ADU47005.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47005.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU47005.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits
CC       weak glutamate--cysteine ligase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01609, ECO:0000256|SAAS:SAAS01123684};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2
CC       family. YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609,
CC       ECO:0000256|SAAS:SAAS00994483}.
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DR   EMBL; CP002343; ADU47005.1; -; Genomic_DNA.
DR   RefSeq; WP_013491326.1; NC_014830.1.
DR   STRING; 710696.Intca_0457; -.
DR   EnsemblBacteria; ADU47005; ADU47005; Intca_0457.
DR   KEGG; ica:Intca_0457; -.
DR   eggNOG; ENOG4106PVI; Bacteria.
DR   eggNOG; COG2170; LUCA.
DR   HOGENOM; HOG000220943; -.
DR   KO; K06048; -.
DR   OrthoDB; 991285at2; -.
DR   BioCyc; ICAL710696:GH9U-469-MONOMER; -.
DR   Proteomes; UP000008914; 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;
DR   PRODOM; E6S8N6.
DR   SWISS-2DPAGE; E6S8N6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916638}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916648, ECO:0000313|EMBL:ADU47005.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916623};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT   COILED       67     87       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   374 AA;  41148 MW;  1A94C2245ADEF72F CRC64;
     MVRTVGVEEE MLLVDVRNGR PKSVSGQLVL RAAMQQQAVA GLGVHGALEG EFQQQMIETH
     TAPVESLEDL EREVRHWRTE ANSAARQVGS SVAALATSPL PVTPIPVEST RYAWMHDRYQ
     IVAKQHLTCG LHVHVAIGSD EEGVGVLDRI RVWLPVLLAL SGNSPFWNGE ATGFASWRSQ
     SFGRWPSNGP TEIFGSAAAY HRMVRDMTMS SVILDEGMVY FDARLSQHYP TVEIRVADVC
     LRASDAVLLA ALCRGLVETA ARDWARSVPV PDVPTTMVRL ATWQAAREGT EGRLLDPFTS
     RPRLAWDVVD RLVEYVAPAL SEAGDVELVK EGLERIRTRG NGAQLQTRTM ERTGQLIDVV
     AHAVRVTAGQ EEDD
//

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