ID C5AZ65_METEA Unreviewed; 286 AA.
AC C5AZ65;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Glutamine amidotransferase-like protein {ECO:0000313|EMBL:ACS41377.1};
DE EC=6.3.5.2 {ECO:0000313|EMBL:ACS41377.1};
GN OrderedLocusNames=MexAM1_META1p3666 {ECO:0000313|EMBL:ACS41377.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS41377.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS41377.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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DR EMBL; CP001510; ACS41377.1; -; Genomic_DNA.
DR RefSeq; WP_003603442.1; NC_012808.1.
DR AlphaFoldDB; C5AZ65; -.
DR STRING; 272630.MexAM1_META1p3666; -.
DR KEGG; mea:Mex_1p3666; -.
DR eggNOG; COG0518; Bacteria.
DR HOGENOM; CLU_065056_0_0_5; -.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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:ACS41377.1}; Ligase {ECO:0000313|EMBL:ACS41377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT DOMAIN 52..207
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 286 AA; 29653 MW; 67614E60785A8F16 CRC64;
MTNAMLRLLI ADGNDRDGRA KREAAVGQTT SQAFASVVAD LAPEAACTLV NPADAEAAIG
SDLAGFDGMV LTGSTLRLAD DGPAVRRQLD LMRAALEAGL PVFGSCWGMQ VAAAIAGGDV
GENPRGPEYG FARRLTATGD GAVHPLLAGR APAWDAPAIH LDAVVGAPSG ARVLAANAML
DVQAIEIRYG RGLFWGTQYH PETDLDELAA MLRLSADAVV SAGLAADHAA VEAYAGEISD
LDGSEGATRR HRAWRLGIGA DVLESTQRRR EIGNFLASLS TARGVE
//
