ID   D9VSL0_9ACTN            Unreviewed;       359 AA.
AC   D9VSL0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFL18811.1};
DE   Flags: Fragment;
GN   ORFNames=SSNG_06063 {ECO:0000313|EMBL:EFL18811.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18811.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL18811.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL18811.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00029283};
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DR   EMBL; GG657750; EFL18811.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9VSL0; -.
DR   STRING; 253839.SSNG_06063; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:InterPro.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.590.20; -; 1.
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   NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR   PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR   PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE   3: Inferred from homology;
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         359
FT                   /evidence="ECO:0000313|EMBL:EFL18811.1"
SQ   SEQUENCE   359 AA;  39135 MW;  8CDECCB14FF78CAA CRC64;
     MMDVEGAHGR GAPRRRGRAS VTAPRMAARP TGRCRALGKE DPMDVLTMGV EEEFHLVDRD
     SRAPVNRAPE VIGELAAELG DQVQAEFYDT QVEVCTLPAA DRDDLRRQLV RLRCSVAEAA
     ARARCLAVAS GSPVVPPQEP LTITDNPRYR LMASRFPGLL GPYRLVCGCH VHVGCLDRGR
     ALALANQMRP WLPALQSITG NSPFVCGRDT GLDSWRSVAY SDWPTVGPPP LLDEPQYLEY
     VDGLVAAGVL LDRRMVYWHA RPSEHVPTLE IRIADVNADL DTVVLTALLV RGLASALLEE
     VDAGVPPPEP PERVLRAAHR LAARYGIDGP GLDVWTGGRA PARMLVDRLV ERAAPGLER
//