ID A0A0J8DE85_CLOCY Unreviewed; 242 AA.
AC A0A0J8DE85;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative glutamine amidotransferase {ECO:0000313|EMBL:KMT22524.1};
GN ORFNames=CLCY_10c00690 {ECO:0000313|EMBL:KMT22524.1};
OS Clostridium cylindrosporum DSM 605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT22524.1, ECO:0000313|Proteomes:UP000036756};
RN [1] {ECO:0000313|EMBL:KMT22524.1, ECO:0000313|Proteomes:UP000036756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 605 {ECO:0000313|EMBL:KMT22524.1,
RC ECO:0000313|Proteomes:UP000036756};
RA Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT HC-1 (DSM 605).";
RL Submitted (JUN-2015) 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:KMT22524.1}.
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DR EMBL; LFVU01000007; KMT22524.1; -; Genomic_DNA.
DR RefSeq; WP_048569938.1; NZ_LFVU01000007.1.
DR AlphaFoldDB; A0A0J8DE85; -.
DR STRING; 1121307.CLCY_10c00690; -.
DR PATRIC; fig|1121307.3.peg.73; -.
DR Proteomes; UP000036756; 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:KMT22524.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036756};
KW Transferase {ECO:0000313|EMBL:KMT22524.1}.
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 242 AA; 26911 MW; 088F07E2358C06FD CRC64;
MKLPIIGISG DLSNTKFFLD FWTKRAGVND AYIQSVSRSS GLPIMLPVTD NLNVSQLIAS
IDGLILTGGK DVSPALYGED SLSLLRETKP ERDAFEMALL KEAIIQNKPI LGVCRGMQLI
NIAFGGTMLQ DVSYDESIKI QHFQQTDSIF PIHNIKVKEN SILHSILGSE SRVNSIHHQA
IKKLSPDFIA TAWASDGVIE GIEKKGDEFI LGVQWHPEMM SETDANMKKL FDRFIEACKR
CM
//
