ID A0A257TRI3_9BACT Unreviewed; 473 AA.
AC A0A257TRI3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glutamate-ammonia ligase adenylyltransferase repeated domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7Z63_01670 {ECO:0000313|EMBL:OYV87917.1};
OS Ignavibacteriae bacterium 37-53-5.
OC Bacteria; Ignavibacteriota.
OX NCBI_TaxID=1970532 {ECO:0000313|EMBL:OYV87917.1, ECO:0000313|Proteomes:UP000225652};
RN [1] {ECO:0000313|EMBL:OYV87917.1, ECO:0000313|Proteomes:UP000225652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37-53-5 {ECO:0000313|EMBL:OYV87917.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYV87917.1}.
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DR EMBL; NCBO01000077; OYV87917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257TRI3; -.
DR Proteomes; UP000225652; Unassembled WGS sequence.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR InterPro; IPR023057; GlnE.
DR InterPro; IPR005190; GlnE_rpt_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF03710; GlnE; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT DOMAIN 79..316
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 343..472
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT NON_TER 473
FT /evidence="ECO:0000313|EMBL:OYV87917.1"
SQ SEQUENCE 473 AA; 53830 MW; E72D5A5C43E3BCF0 CRC64;
MDAAAKENIS RLLQKIFELT VNSGAAINPA EFTDRLEQST GVLPDQFMTL NNFERFLAAT
PNSASVLSDL SRDAKLFSDF LKIISTSQYL TDILVRHSSY FRFLFSPAGI ESPVRPDFLL
NELSNQVSIY REASHKNDFV RRIYKREILR IGGRDICGRD NLEATTLQIS QLAECMLRIS
FSIAAEEVKA KRGQLLAPVS CIALGKFGGN ELNYSSDIDL MFLYSEGKGQ GDLEASEEAN
YFASELMKHL TAESAEGHLY RVDLRLRPDG TSGAAAQSLD GMIAYYESRG ELWERQMLIK
ARHVAGDEAL SNTFLNHLRP FIYPRTWLEN PIDEIPRMKI RIETANPNEY NIKIRRGGIR
DIEFVVQALQ LLNGGANPEI QTGNTLRAIK LLAKNGILNK REAALLSNAY KFYRLVEHRL
QLFSNMQTHT LPSDMIEFRN LSKRCGYKNE RKFRNELFGY FDEVSELFNN VFR
//
