ID A0A1E5Q8B8_9PROT Unreviewed; 257 AA.
AC A0A1E5Q8B8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase {ECO:0000313|EMBL:OEJ67549.1};
GN ORFNames=BEN30_08935 {ECO:0000313|EMBL:OEJ67549.1};
OS Magnetovibrio blakemorei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetovibrionaceae; Magnetovibrio.
OX NCBI_TaxID=28181 {ECO:0000313|EMBL:OEJ67549.1, ECO:0000313|Proteomes:UP000095347};
RN [1] {ECO:0000313|Proteomes:UP000095347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV-1 {ECO:0000313|Proteomes:UP000095347};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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:OEJ67549.1}.
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DR EMBL; MCGG01000021; OEJ67549.1; -; Genomic_DNA.
DR RefSeq; WP_069957702.1; NZ_MCGG01000021.1.
DR AlphaFoldDB; A0A1E5Q8B8; -.
DR STRING; 28181.BEN30_08935; -.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000095347; 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};
KW Hydrolase {ECO:0000313|EMBL:OEJ67549.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095347}.
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 257 AA; 27927 MW; CFB8F13293BA2B44 CRC64;
MTHDSHTDLI TPVIGIPLDS DTGGADQYSK FPWYALRHNY ISAVVKAGGL PLLLPHEPSL
LDIYLDDIDG LLITGGNFDV DPALYGQTIV HDSVTTKDDR TSFEMGMLQG ALKLDVPILG
ICGGQQLIHV ALGGTLVQHI PDEFPGCLAH EQPNPRDQVS HNVEITKGTL LDQIIGQPHI
QVNSAHHQAA RDEPAGVRIN ARAPDGVIEG CEAINMSFCL GVQWHPEFEI TPADSRIMAA
FVEAARVYAI DRDNSYD
//
