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Database: UniProt
Entry: R5WBJ4_9FIRM
LinkDB: R5WBJ4_9FIRM
Original site: R5WBJ4_9FIRM 
ID   R5WBJ4_9FIRM            Unreviewed;       227 AA.
AC   R5WBJ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Class I glutamine amidotransferase {ECO:0000313|EMBL:CCZ93161.1};
GN   ORFNames=BN751_02285 {ECO:0000313|EMBL:CCZ93161.1};
OS   Coprococcus eutactus CAG:665.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=1263071 {ECO:0000313|EMBL:CCZ93161.1, ECO:0000313|Proteomes:UP000017949};
RN   [1] {ECO:0000313|EMBL:CCZ93161.1, ECO:0000313|Proteomes:UP000017949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:665 {ECO:0000313|Proteomes:UP000017949};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ93161.1}.
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DR   EMBL; CBAW010000096; CCZ93161.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5WBJ4; -.
DR   Proteomes; UP000017949; 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   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:CCZ93161.1}; Transferase {ECO:0000313|EMBL:CCZ93161.1}.
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   227 AA;  26089 MW;  36AAF49853307DD9 CRC64;
     MLRALITQRE GHNMYGKSTD VLEAAYVEFY ESMGIRLLPV SNFTKDFDAV VDQQFDLLIV
     TGGGTLHPRH YLEPHNAELQ PRRDAMEEQL IMYCVHNNIP VIGVCRGMQH INALFGGKIS
     YSARFKVPRP RGVDHLARIV NTDRYVKINN FHSDCVYLEN MSTMFYPIVV DEENESVEAF
     VSPAMSILAF QWHPERIFES EEGRLFSRHL IQDFLGIPRD DAKPAID
//
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