ID A0A0S8ABC8_9GAMM Unreviewed; 723 AA.
AC A0A0S8ABC8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPJ95946.1};
DE Flags: Fragment;
GN ORFNames=AMJ55_02870 {ECO:0000313|EMBL:KPJ95946.1};
OS Gammaproteobacteria bacterium SG8_15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703403 {ECO:0000313|EMBL:KPJ95946.1, ECO:0000313|Proteomes:UP000053644};
RN [1] {ECO:0000313|EMBL:KPJ95946.1, ECO:0000313|Proteomes:UP000053644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_15 {ECO:0000313|EMBL:KPJ95946.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ95946.1}.
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DR EMBL; LJNL01000036; KPJ95946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8ABC8; -.
DR Proteomes; UP000053644; 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; 1.20.120.1510; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.10.4050.10; Glutamine synthase adenylyltransferase GlnE; 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; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
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 47..291
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 314..453
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 571..718
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT NON_TER 723
FT /evidence="ECO:0000313|EMBL:KPJ95946.1"
SQ SEQUENCE 723 AA; 82384 MW; E2C6A27424FBA589 CRC64;
MSDLLTDFLL LHPESVQQRV QRDWEALMHG LEDQAWIESS LLPHKAELLR VWALSEFASK
LCATQPAILA GLINSNDLFR RYPDGHYAHS LRHQLAHLET EFDLHQCLRR FRNREMLRIA
WRDICGHASL MQTMHDLSSL ADACIAETLQ VLHHWLAKEL GQPQDNQGNS QRMIVVAMGK
LGAYELNYSS DIDLIFIYPE PGETGNATRT VSNEQFFTRV SKQLIAALDR RTGDGFVFRV
DMRLRPFGES GPLVASLEAL ENYYQSHGRE WERYAFIKAR VVSGDPEPTN ELVQMLRPFV
YRRYLDYGAY ESLREMKQLI VAEVERKGLK DNIKLGAGGI REIEFIGQAF QLIRGGRDPE
LQQKQILHTL DVLGLKQQLP DYVVKELKDA YQFLRTTEHR LQQVRDAQTH QLPKDADERA
CIALAMGFDS WEAFYQKLQI HRQRVRNHFD QVFESPQISQ SDEVDRSLQL KQLWLQKLEQ
DKAEVLLGEL GYEHPANVLD LLKSLGSMAT TRSLSRTGRQ RLDALMPLLI AAVASKKNNH
DVLKRVLALI QAISRRSSYL ALLLENPMAL SQLIKLCAAS PWIAHQLKQH PLLLDELLDP
RALYDPPTRE ELGQDLDRRL AHIAADDLEQ QMDALRHFKQ ANVLRVAAAD VSTYIAETVV
ARALDMAWSH MTQRHGAPAA GDDTSARQHF AVVAYGKLGG IELSYGSDLD LVFLYDADPN
GFT
//
