ID A0A136L7D3_9BACT Unreviewed; 382 AA.
AC A0A136L7D3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamine synthetase adenylyltransferase {ECO:0000313|EMBL:KXK17534.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:KXK17534.1};
DE Flags: Fragment;
GN ORFNames=UZ18_ATM001001076 {ECO:0000313|EMBL:KXK17534.1};
OS Armatimonadetes bacterium OLB18.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK17534.1, ECO:0000313|Proteomes:UP000070351};
RN [1] {ECO:0000313|EMBL:KXK17534.1, ECO:0000313|Proteomes:UP000070351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB18 {ECO:0000313|EMBL:KXK17534.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-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:KXK17534.1}.
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DR EMBL; JZQX01000113; KXK17534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136L7D3; -.
DR STRING; 1617424.UZ18_ATM001001076; -.
DR Proteomes; UP000070351; Unassembled WGS sequence.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ECO:0000313|EMBL:KXK17534.1}; Transferase {ECO:0000313|EMBL:KXK17534.1}.
FT DOMAIN 106..215
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 240..371
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXK17534.1"
SQ SEQUENCE 382 AA; 42888 MW; 09C9A96E63938FF2 CRC64;
YESLLVNKDS LRRVERIAVA SPAAIDSCVR DVGLTEAILS GEIEEDLDCE SFDFKSVGEG
SLAEIAAAAR RCIDRLKIKW TLAPDFPVWD ALSRVYDGLV GSVANRLNAG FDVLALGSYA
NQSAGFVSDL DLMFLAEDSG PESAHEKQAQ AFLGEMRELR SFGIPVNCDL RLRPEGRHGM
LVRTYEGFSA YELGAMDLWE RFALGECRTV WGSSRAFELV VKAAYALPIT PERLQELLAM
KKRIETERVT VKYRTRNVKL GVGGLSDIEW FVHLHEMRYP TATEAGTLHR LDDRLRQLAR
ARLINAVELD ALSEGLRHLL TLRERLALLG LTTDIVPENP DRLDRLAWTF GFERGNEFLA
KHEHITSAVR LIFLEGIERL RA
//
