ID A0A2A9CU33_9ACTN Unreviewed; 397 AA.
AC A0A2A9CU33;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=ATK74_2512 {ECO:0000313|EMBL:PFG17934.1};
OS Propionicimonas paludicola.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Propionicimonas.
OX NCBI_TaxID=185243 {ECO:0000313|EMBL:PFG17934.1, ECO:0000313|Proteomes:UP000226079};
RN [1] {ECO:0000313|EMBL:PFG17934.1, ECO:0000313|Proteomes:UP000226079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15597 {ECO:0000313|EMBL:PFG17934.1,
RC ECO:0000313|Proteomes:UP000226079};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG17934.1}.
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DR EMBL; PDJC01000001; PFG17934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9CU33; -.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000226079; 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:PFG17934.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000226079}.
SQ SEQUENCE 397 AA; 42781 MW; 328A9E0AC63506DD CRC64;
MPSRSRRSPF STLPGRASEQ RTFGVEEELL VVDATTLRPV PRGEAIVASA ETSAAGHRLT
TEFKREQVEV VNPPQTTLDG QLAAIRTGRA IADAAAAQHD ARTVPLATSP WPLTSTLVDH
PRYAEMAGRF ALTAVDQLTC GFHVHVGVAS DQEGVAALDR IRGWLPVLLA LSANSPLWMG
MDTGFASYRY QVWSRWPTAG PSELFGSADG YRRHCAELLD TGVPLDEGML YFDARLSNAF
PTIEVRVADV CLQPTHAAGL AAIIRALVET AVREWQAGRA PAAVSAAVLR TWSWQASRFG
LTRSLVSPIT RSPAPAAEVV GQLLAAIDPV LAEFGEREPV AELIQELLAG GSGAERQREF
RASATDTHNR RDLRTVVRRA LLEAGGEAAD GRLELLS
//
