ID A0A3S2U9B3_9RHOB Unreviewed; 384 AA.
AC A0A3S2U9B3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=DXV76_17375 {ECO:0000313|EMBL:RVT82246.1};
OS Rhodobacteraceae bacterium CCMM004.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT82246.1, ECO:0000313|Proteomes:UP000287438};
RN [1] {ECO:0000313|EMBL:RVT82246.1, ECO:0000313|Proteomes:UP000287438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM004 {ECO:0000313|EMBL:RVT82246.1,
RC ECO:0000313|Proteomes:UP000287438};
RA Zhang Z.;
RT "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT culture.";
RL Submitted (JAN-2019) 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|HAMAP-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:RVT82246.1}.
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DR EMBL; RZWH01000006; RVT82246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2U9B3; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000287438; 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; 3.30.590.20; -; 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:RVT82246.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000287438}.
SQ SEQUENCE 384 AA; 43492 MW; EE7A474F4F9432D7 CRC64;
MPHRSEKLPL GLEEEYLLID PETRALAARQ PKGFMEDCRK RLGGKVMYEF LQCQVEIGTG
VCATIPQARS EILELRAIIS ETAREHGMAM IAASTHPWAH WKDQEPVDMD RYRILGAEHR
TLARRMAICG MHVHAGIEDK NLRVELMAQM SYFLPHLLAL SGSSPFWEGA DTGLKSFRPI
IIGDLPRSGF PEVFENWNDW TDMLEDLEVP GLVSDASRIW WDIRPSVRHP TLEIRVCDIC
TWAEDGLTIA ALYQSILAYL CHLRGRNERR RHYRRILLAE NKWRAMRYGV EAQMADFGKR
ELKSVCDLTD ELIELVSPFA EELGCLDEVR HAATICRRGT SSDHQIRVYT EALEGGADEQ
AAKCAVVDWL VEQSAVAQGP AAPA
//
