ID K1Y454_9BACT Unreviewed; 96 AA.
AC K1Y454;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=CobB/CobQ-like glutamine amidotransferase domain-containing protein {ECO:0000259|Pfam:PF07685};
GN ORFNames=ACD_75C01065G0002 {ECO:0000313|EMBL:EKD37620.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD37620.1};
RN [1] {ECO:0000313|EMBL:EKD37620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD37620.1}.
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DR EMBL; AMFJ01031734; EKD37620.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Y454; -.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR004484; CbiA/CobB_synth.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011698; GATase_3.
DR PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00606}.
FT DOMAIN 24..81
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 96 AA; 10956 MW; B810959423531E3A CRC64;
MSKKPQAHGY TIFRVDRNNP FYGLGEEVKG HEFRYSKVLD WQGTDEQLAF TMVRGNGFAG
GRDGLVYNNV LALYTHVHAD GTPQWAENFV SRCCRK
//
