ID   A0A017HHG4_9RHOB        Unreviewed;       928 AA.
AC   A0A017HHG4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:EYD73765.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:EYD73765.1};
GN   ORFNames=Lokhon_00321 {ECO:0000313|EMBL:EYD73765.1};
OS   Limimaricola hongkongensis DSM 17492.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD73765.1, ECO:0000313|Proteomes:UP000025047};
RN   [1] {ECO:0000313|EMBL:EYD73765.1, ECO:0000313|Proteomes:UP000025047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD73765.1,
RC   ECO:0000313|Proteomes:UP000025047};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (MAR-2013) 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:EYD73765.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APGJ01000001; EYD73765.1; -; Genomic_DNA.
DR   RefSeq; WP_017929431.1; NZ_KK088648.1.
DR   AlphaFoldDB; A0A017HHG4; -.
DR   STRING; 1122180.Lokhon_00321; -.
DR   PATRIC; fig|1122180.6.peg.326; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000025047; 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   GO; GO:0016874; F:ligase activity; 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   Ligase {ECO:0000313|EMBL:EYD73765.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:EYD73765.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000025047};
KW   Transferase {ECO:0000313|EMBL:EYD73765.1}.
FT   DOMAIN          44..274
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          297..438
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          524..765
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
SQ   SEQUENCE   928 AA;  99771 MW;  2CA007D3177D1D7D CRC64;
     MTDLASRLRR APRPFDPDKA AEARALCGWA DPATAELIGG TAGCSPYLAN LMSHESGWLE
     AACADPESMV EAELAGFAGL DAKALGPRLR RAKRRVALIA ALADLGGAWP LEQVTGSLTR
     LADAALQAGL EALIAPEIAR GKLPGMGEDD IATGAGMAIF AMGKMGAFEL NYSSDIDLIC
     LYDETRYEGA DQHEARAVLV RVTRKLAGLI GDITDEGYVF RTDLRLRPDA AVTPVCLSMA
     AAEQYYESVG RTWERAAWIK ARPCAGDLSA GARFVDTLRP FVWRRHLDFH AIRDAHDMRL
     KIRDHKGLGG ALQLPGHDVK LGRGGIREIE FFTQTRQLIS GGRDASLRLR GTIEGLDRLA
     QAGWIETGTA EALSRHYRAH REVEHRVQMV GDQQTHKLPS SEEGFARLAA FMDRDEADLK
     SELTERFEQV HALTEDFFAP GHTESTVPDF GREVTARWPG YPALRSDRAV EIFDRLRPEI
     LKTLGEAARP DEALAQFDAF LAGLPAGVQL FSLFEANPQL TRLLVDICAT APGLAQYLSR
     NSGVLDAVIG GGFFADWPGV AALRSDLADR LARQPDHEAR LGAARVWAKE IHFRIGVHHL
     RGLIDAATAG REYAELAEAV VSALVPVVID EIARRHGPPP GRGLSVLAMG SLGAGRLGSS
     SDLDLIVIYD AGGVEASEGP RPLAARTWYA RFTQGLITAL TAPMPDGRLY EVDMRLRPSG
     RQGPVATALP AFRAYQQDEA WTWEHLALTR ARAVAGEPGL GAEIETFRRE LIAQKAGGDT
     VAADLAAMRA RLAEARPGGE GWNLRDGPGR LQDVELFAQS LALRAGSAAR EVPAQIAAGH
     GAGLIDEEGA AVLTETGDLL RRVQCVARLL TGGGPLPETP AEGGARLLLR ESGCDTLDDL
     RRALDAASAR AEGVIAQALR GAEAGETR
//