ID D5UID4_CELFN Unreviewed; 382 AA.
AC D5UID4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Cfla_2591 {ECO:0000313|EMBL:ADG75479.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75479.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG75479.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(2010).
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000256|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:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
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DR EMBL; CP001964; ADG75479.1; -; Genomic_DNA.
DR RefSeq; WP_013117812.1; NC_014151.1.
DR AlphaFoldDB; D5UID4; -.
DR STRING; 446466.Cfla_2591; -.
DR KEGG; cfl:Cfla_2591; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_1_11; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000000849; 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 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;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:ADG75479.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000000849}.
SQ SEQUENCE 382 AA; 42064 MW; 5F2D0965F5559C6A CRC64;
MAAPVALPFA RSERSTVGIE WEVALVDADS GDLRQAAEAI FEAVRPADGS DHPHITSELL
LNTVEVSSGK CRTVGEAGED LRRALDEVAA AARPLRIELM GGGTHPFASW ATQRVTDKQR
YATLIDRTQW WGRQMLIFGV HVHVGIEDRD KVLPLSRAML TVLPHIQSLS ASSPFWGGKD
TGYASNRALL FQQLPTAGLP PQLERWDQLE QYVGDMMHTG VIDQVNEVRW DVRPAPRFGT
LEMRIADGAA SLLEVTAISA FTHCLVEHFS SMIDAGEPLP TMPPWFVQEN KWRSARYGMD
AIVITNAAGD EELVTDSVAR WLGELAPVAE RLGCTAELDQ VRVILRRGAS YQRQRAVARR
HAGELEPVVR SLVAELAAGR PL
//
