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Database: UniProt
Entry: A0A1M3BIP8_9ACTN
LinkDB: A0A1M3BIP8_9ACTN
Original site: A0A1M3BIP8_9ACTN 
ID   A0A1M3BIP8_9ACTN        Unreviewed;       259 AA.
AC   A0A1M3BIP8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJU84134.1};
GN   ORFNames=BGO11_20890 {ECO:0000313|EMBL:OJU84134.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU84134.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU84134.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU84134.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJU84134.1}.
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DR   EMBL; MKSH01000093; OJU84134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3BIP8; -.
DR   Proteomes; UP000184118; 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: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}.
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   259 AA;  27984 MW;  E7F9B4A8D947D7CB CRC64;
     MSADDHADTP PVIGITGRRY PAGIVHGAEM QAAMSGIWIE AFYTSYSERL GALGAIPLYV
     TRQADPAALL ARLDGVVLAG GIDVDPRLYG SQPTEHSTVL DPAQDEWEIA LTRLAVERGV
     PVLGTCRGHE LLNVAFGGTL REHLEGLSSP HHRRIIYPLQ DRGHRVETAT DSKLRELYGP
     TAEVNSFHHQ AVDRLGEGVR ACAYAEDEVI EAIEIEGADA IGVQWHPEFV EDAEPILGWL
     VERARAFAAA RAIGAGEAS
//
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