ID A0A258GV97_9PROT Unreviewed; 945 AA.
AC A0A258GV97;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:OYX48685.1};
GN ORFNames=B7Y90_09660 {ECO:0000313|EMBL:OYX48685.1};
OS Alphaproteobacteria bacterium 32-64-14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1970492 {ECO:0000313|EMBL:OYX48685.1, ECO:0000313|Proteomes:UP000215897};
RN [1] {ECO:0000313|EMBL:OYX48685.1, ECO:0000313|Proteomes:UP000215897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-64-14 {ECO:0000313|EMBL:OYX48685.1};
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:OYX48685.1}.
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DR EMBL; NCEM01000019; OYX48685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258GV97; -.
DR Proteomes; UP000215897; 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; 1.20.120.1510; -; 1.
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; 2.
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:OYX48685.1}; Transferase {ECO:0000313|EMBL:OYX48685.1}.
FT DOMAIN 30..262
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 288..427
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 540..772
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 798..928
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 945 AA; 102776 MW; F15211A4C82D5E98 CRC64;
MAIQLDTLGI APVTGARGDL RGALELAPRH SDHIARMVAR RPDVAEAILA SDAEAVVDQA
VQDILAAGAM AGPLDAPMRQ MRRAKEAAQL AISIADLCCA WTLDAVVERL TRLADAATQA
ALSLAIRTSW AAGHLGETRD SDAMPGLFTL AMGKMGAREL NYSSDIDLIV LFDLDLLPVS
GPRVKEGMTR LTRDFVRILE ERTADGYVFR TDLRLRPDPA STSPAISTQF ATGYYESVGQ
NWERMAHIKA RVCAGDAAAG KDYLSELQPY VWRRHLDYWA IADIHSIKRQ IHAHGGHAEL
TSRDFDVKLG RGGIREIEFF TQVQQLILGG RMPHLRLPGT KAALQVTANE QIVDPDVVND
LCRAYDYLRA IEHRVQMLND EQTHRIPVVP ERREAVSRLA GYGDTALFEA DISRVRARVH
GAYSDLFAAE ERLSGEAGNL VFTGVDDDPG TVATLTTLGF SDPSRVIHTF QQWHRGAIPA
TRSARAQQLL TSLGPRLLEA MSKAGEPDIA FDRFQEFFSG LNSGVQVMSL MLAEPGLTRD
VIQTMAFAPK LAADLARRPA LMEAMLERSF STPAHLDEAG SRALRLVDNL ERAEGFEAKL
NTARRFHREE AFRIGYQLLR GAIGAAEAGV AYADLADACV GGLAEVCECE ILAKFQGEIG
GWSVCALGKF GGRELTATSD LDLMLVYEPA NDGSVQLATR FVQRLVAALS APTEEGLLYE
VDMQLRPSGR AGPVAVRMSS FERYYREEAW TWEFMALTRI RPVAGDTDLG RRIVESARKA
LQAKSGDPKI TEDIGDMRRR MARERTARSM WDVKLAPGGL VDIEFVTQHA ILAAAARTPG
AVQPGSLAAI KMLASSGHLA AGDAALMIDA LGLQLNLQQA LRIAAGDGFE PDAASDGLKV
WLAKHLGFKD FPALAARLAD IQAQVAALRT RKLGPLSTEE PGEAV
//