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Database: UniProt
Entry: A2C9J8_PROM3
LinkDB: A2C9J8_PROM3
Original site: A2C9J8_PROM3 
ID   A2C9J8_PROM3            Unreviewed;       247 AA.
AC   A2C9J8;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Glutamine amidotransferase class-I {ECO:0000313|EMBL:ABM78158.1};
GN   OrderedLocusNames=P9303_14111 {ECO:0000313|EMBL:ABM78158.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78158.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM78158.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78158.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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DR   EMBL; CP000554; ABM78158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C9J8; -.
DR   STRING; 59922.P9303_14111; -.
DR   KEGG; pmf:P9303_14111; -.
DR   HOGENOM; CLU_054974_3_1_3; -.
DR   BioCyc; PMAR59922:G1G80-1217-MONOMER; -.
DR   Proteomes; UP000002274; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW   ECO:0000313|EMBL:ABM78158.1}; Transferase {ECO:0000313|EMBL:ABM78158.1}.
FT   DOMAIN          25..189
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   247 AA;  27310 MW;  CEE89F8BB928DE78 CRC64;
     MTPLFVVQHL ERETPGLFQD LAQQHGMAVQ VIRVDLGEPL PSLVKGDGLL VLGGPMGVAD
     LYKPAFPWLE DEVLLIQQAL EHQIPFVGVC LGAQLLAHAA GGGVEPLLGG DPPRPLAEVG
     WAPITSTLEA ANQSLITSLM QPLDVLHWHG DRIILPETAN VLATSVRCRE QLFRIGPLAY
     GLQFHLEVED QDVFRWIAED NDFICGALGE NAADILRDQQ RLYSSSSRPR RLKLLADLFR
     ELWPSYF
//
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