ID K2CRY2_9BACT Unreviewed; 163 AA.
AC K2CRY2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=Aspartyl/glutamyl-tRNA amidotransferase subunit B {ECO:0000313|EMBL:EKD88496.1};
DE Flags: Fragment;
GN Name=gatB {ECO:0000313|EMBL:EKD88496.1};
GN ORFNames=ACD_34C00501G0003 {ECO:0000313|EMBL:EKD88496.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD88496.1};
RN [1] {ECO:0000313|EMBL:EKD88496.1}
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:EKD88496.1}.
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DR EMBL; AMFJ01012844; EKD88496.1; -; Genomic_DNA.
DR AlphaFoldDB; K2CRY2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.410; -; 1.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000313|EMBL:EKD88496.1}.
FT DOMAIN 9..158
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD88496.1"
SQ SEQUENCE 163 AA; 17662 MW; 51638A469BAEF7A4 CRC64;
IAAECEVSDF FESCVKALKN PNPKSVAAWI TGELFAWLNL SGKDFVEIKV TPSGLAELID
LVQEGVINQN TAKAVFVKML ETDKSAREIV KAEGLAQTSD GDAIARLVSE VIGAYPDELE
SYKSGKETLS NWFFGQVMKA AGGKANPAVL KSELEKQLQQ HKS
//
