ID   A0A1S9MHA4_9MICC        Unreviewed;      1003 AA.
AC   A0A1S9MHA4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:OOP64657.1};
GN   ORFNames=BMF89_02745 {ECO:0000313|EMBL:OOP64657.1};
OS   Arthrobacter sp. SRS-W-1-2016.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1930254 {ECO:0000313|EMBL:OOP64657.1, ECO:0000313|Proteomes:UP000190514};
RN   [1] {ECO:0000313|EMBL:OOP64657.1, ECO:0000313|Proteomes:UP000190514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS-W-1-2016 {ECO:0000313|EMBL:OOP64657.1,
RC   ECO:0000313|Proteomes:UP000190514};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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:OOP64657.1}.
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DR   EMBL; MTPV01000012; OOP64657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9MHA4; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000190514; 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; 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:OOP64657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190514};
KW   Transferase {ECO:0000313|EMBL:OOP64657.1}.
FT   DOMAIN          76..327
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          348..492
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          597..836
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          875..998
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1003 AA;  109595 MW;  C8551FDDE0123841 CRC64;
     MSLARRLISA GFSDLEKGER FLAARELDGI DQETIFAGLH LSANPDTALQ SLVRLIEKHP
     SLRQLAGEHP DRSEPLYRLL GASEALGEFL IRHPEHLDVF DVRVSPEPLS ADAGELRRKL
     LRSVKADPNS PRPVAATTGA SAYAALRTAY RRGLTELAIK DLCAASPQDF MPAVGAELAD
     LAGAAIEAAL AVARAEAAAT FDPADIAGVG LAVIGMGKCG ARELNYISDV DVIYVIEAPD
     LEDAEAATIG TALAAGISRA ISSTGTEPGL WEVDANLRPE GKSGPLVRTL PSHLSYYAKW
     AESWEFQALL KARTIAGDRD LGSRYEKAVQ PLVWASAGRE GFVESVQAMR RRVTNNIAPA
     EEQRQIKLGP GGLRDVEFTV QLLQLVHGKS DETLRCRDTT SAIAALSAGG YIGRVDAAAF
     DAAYRYLRVL EHRIQLFQMR RTHLMPTSQE SLRFLAKAVL GPFSTGRPHP DALIETWQKT
     KRSVRELHDR IFYRPLLNTA AKLSTEDARL TPEAAQGRLA ALGYRDPQGA MRHIEALTAG
     VSRRAALQRQ LLPILLGWLA EGVDPDAGLL AFRRVSEALG TTHWYLGMLR DSQAAAERLC
     HVLSNSRLIA DLLEVSPESV AWLGADKELL PLSFEAQWQE IQSKMSRHAD PANAMRLIRL
     IRRREILRIA IADSAGLLEQ DAVGAALADA DRAAVLGALH VAEAIVGSDG PLKTQVLVVA
     MGRQGGREIG YGSDADVMYV HRALPGASEA EAQQQALAIV GHISTLLTQP LKPAILAERV
     LAVDADLRPE GKNGAMVRSL ESYAEYYRRW SLIWEAQALL RAQPMAGNDE LAAEFVRLIN
     PIRYPESLPE TDVREIRRVK ARVESERLPR GADPARHVKL GRGGLSDVEW LVQLLQLQHA
     GKQPQLRTTS TLQALDAIES LDLIAKGDIV LLRKAWRLAS RIRSANVICT GRASDLLPAS
     RRDLEAVARW CGYAPGQAAV FEEDYLRLSR RTRAVFEKDF YGQ
//