ID U4UVY5_9RHOB Unreviewed; 252 AA.
AC U4UVY5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Putative glutamine amidotransferase {ECO:0000313|EMBL:ERL97989.1};
GN ORFNames=HIMB11_01301 {ECO:0000313|EMBL:ERL97989.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL97989.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL97989.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL97989.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERL97989.1}.
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DR EMBL; AVDB01000004; ERL97989.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UVY5; -.
DR STRING; 1366046.HIMB11_01301; -.
DR PATRIC; fig|1366046.3.peg.1308; -.
DR eggNOG; COG2071; Bacteria.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000016848; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01745; GATase1_2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR Pfam; PF07722; Peptidase_C26; 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:ERL97989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW Transferase {ECO:0000313|EMBL:ERL97989.1}.
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 252 AA; 27584 MW; AA9194211294A035 CRC64;
MKRPVVGVVG NQYMINDQYP VHAAGRMTTW AVSHVSNCAP MIVPTDPEIA SVSELIEICD
GFVFTGGRPN VHPEEYGEVA TEAHGDFDRG RDAIALGIIR ACVERGQPIF GICRGFQEVA
VAMGSTLHPE IRDLPGRDNH RMPPDGTMEE KFALRHVVTV SENGPFYNVF GATEVMTNTL
HGQGIERAGD RIVIDGYAPD GTPEAIYVKD APGFTLSVQW HPEWNADQDP VSRPLFQAFG
QAAYDYAKAR TS
//
