ID A0A3N1Q9V0_9MICO Unreviewed; 848 AA.
AC A0A3N1Q9V0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=EDF46_0105 {ECO:0000313|EMBL:ROQ40744.1};
OS Frondihabitans sp. PhB188.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=2485200 {ECO:0000313|EMBL:ROQ40744.1, ECO:0000313|Proteomes:UP000269803};
RN [1] {ECO:0000313|EMBL:ROQ40744.1, ECO:0000313|Proteomes:UP000269803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB188 {ECO:0000313|EMBL:ROQ40744.1,
RC ECO:0000313|Proteomes:UP000269803};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:ROQ40744.1}.
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DR EMBL; RJUO01000001; ROQ40744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1Q9V0; -.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000269803; Unassembled WGS sequence.
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; 3.30.1490.270; -; 1.
DR Gene3D; 3.30.590.20; -; 1.
DR Gene3D; 3.40.50.11290; -; 1.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR025841; CP_ATPgrasp_2.
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; PTHR34595; BLR5612 PROTEIN; 1.
DR PANTHER; PTHR34595:SF2; SLL1039 PROTEIN; 1.
DR Pfam; PF14403; CP_ATPgrasp_2; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:ROQ40744.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000269803}.
FT DOMAIN 445..817
FT /note="Circularly permuted ATP-grasp type 2"
FT /evidence="ECO:0000259|Pfam:PF14403"
SQ SEQUENCE 848 AA; 90969 MW; 9F97894757DFE2E5 CRC64;
MSAELTLGAE EELHLIDLET KRLSARAPQL LSKLPPDKYG AELQRTTVET NVPVVTNLTD
LRREILALRR DLVEVATAND LAIAAAGTAP RSEFADFELT TTGRYGRMQE QYRMLVDEQL
ICGLQVHVGV SDRDLAVQIM GRVAPYLPGL LALSASSPFW NGQDTGYASI RSIIWQRWPS
AGATGPMSGA AEYDRMVQDL IGSGVIADAK MAYFDIRPSS HAPTLELRTC DACPIVDDAV
LIAGLFRAAV RKAEIDILDG RPDRQRAAPL HRAAMWQAAR AGLTGELLGL GIHPERLPAA
QAVRSLATSL RPQLEELGDW HDVEGLIEQT LARGNSADRQ RAAFAEHGSL DDVVDQVVKE
THGPAAGDLP TTPTIRGYRF RAGDEAIGPG LRARPAYADV GGYFRTLDAE AIRAKNERRD
EWAQKRGLSF VVDDKLRGFG VDLVPRIVTH HEWKQLAAGL AQRARAIEAF LEDAYGSRRI
VADGVLSEAQ VVDASGWRVE ASLLPTGTVR APVQGFDLIR NEFGGWRVLE DNVRSPSGAA
YAVAVRHLLD EVVPEAPRPA GLLNPETVFA LLRETLLAHS TNPEPVGAVL SSGPGSGAWF
EHQALAEGAG LLLVTADDLA VDGHRVRHAA TGEVIDALYL RMDGEVLELA TPADPDLGAR
IIDVAATGDV FLANAPGNGL ADDKAMYVAV PDLIEYYLDE KPKLESVPTY RLSDEAEKLS
VLDRVGELVT KPVDGEGGHG VLIGPSANAA EVAARRAEIA ADPARWVAQE VVTLSSHPTL
TATGLEPRHV DLRAFVYLTG VGPTQARLAD FALTRVAPEG SMVVNSSRGG GAKDTWIIGP
DAGSDGEA
//
