ID A0A2R8ABK1_9RHOB Unreviewed; 905 AA.
AC A0A2R8ABK1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000313|EMBL:SPF29592.1};
GN Name=glnE {ECO:0000313|EMBL:SPF29592.1};
GN ORFNames=POI8812_01905 {ECO:0000313|EMBL:SPF29592.1};
OS Pontivivens insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pontivivens.
OX NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF29592.1, ECO:0000313|Proteomes:UP000244932};
RN [1] {ECO:0000313|EMBL:SPF29592.1, ECO:0000313|Proteomes:UP000244932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF29592.1,
RC ECO:0000313|Proteomes:UP000244932};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OMKW01000002; SPF29592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ABK1; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000244932; 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; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
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; 2.
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:SPF29592.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244932};
KW Transferase {ECO:0000313|EMBL:SPF29592.1}.
FT DOMAIN 80..265
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 287..424
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 520..760
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT REGION 427..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 98097 MW; 912A9A0FE720648E CRC64;
MTLTDRITRF PIACDPEKGE RLAEPFTGPL RDLVQGAAGT SNYIAALVGR EAGWLIDVSG
LEPDDAFKRA MALGAGDPAT ALRQAKRRVA LLTALLDLGG VWSTLDVTRA LTRFADMAVW
EAARPGIERE IAKGNLQGGT DGTAGFCVLA MGKMGAGELN YSSDIDLICL FDETRYQPDD
FATARAAFLR VTKGMVRTLA DVTQDGYVFR TDLRLRPDPS VTPVCIAMEA AERYYESAGR
TWERAAFIKA RPCAGDLEAG AAFLKRLQPF KFRRHLDFAA IRDAEDMLDK IRTHKGLAGR
FSVAGHDLKL GQGGIREIEF FAQSRQLILG GRNHDLRGRE TLEVLGALAA TEWIDAERAD
LLSRAYMRLR DVEHRVQMLD DAQTHTLPKS DTQRTKVAAL DGCDDLAAFD REIAELVQTV
HAATAPKQGT ERVAESVAPP PMAEDPDVRR ILDGWHKLPA TRSPRADALL SQLEPEILRR
LSEAGDPMAA LAQFDGFLRG LPAGVQVFSM LASNPPLMAL LVDICAMAPA LAQYLGRNSG
VFDAVLDRGY FGPLPERAAL ETQLREILER SADYESILDD TRRWQKEQHF RIGVHLLRDL
TDTAGAERAY AALAEASVSA LLPAVIAEQA KRHGAPPGNG MCIVGMGRLG SREMTASSDL
DLIMIYDAEP DDLSEGRTPL AAGAYYARLT KRLISALTAP TATGRLYEVD MRLRPSGRQG
PVAVSLSSFR RYQRDEAWTW EHLALTRARA VAGPAELVAA VDVAIADVLA MPRDGAKVAR
DVREMRARLL AARADAAQDR WEIKQGPGRL LDIDLYLQAR KLVGLPADEA VAEMRARLAI
LQSIGRVAFA EGFDPSRAGG ALISLVLGLT GTDDLGALEA VLMDGAALAA QSIEGGLDAI
EAAGP
//
