ID A0A239EJW6_9SPHN Unreviewed; 889 AA.
AC A0A239EJW6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:SNS44568.1};
GN ORFNames=SAMN06295912_106167 {ECO:0000313|EMBL:SNS44568.1};
OS Sphingomonas laterariae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=861865 {ECO:0000313|EMBL:SNS44568.1, ECO:0000313|Proteomes:UP000198281};
RN [1] {ECO:0000313|Proteomes:UP000198281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LNB2 {ECO:0000313|Proteomes:UP000198281};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; FZOS01000006; SNS44568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239EJW6; -.
DR Proteomes; UP000198281; 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 GO; GO:0016874; F:ligase activity; 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; 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:SNS44568.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:SNS44568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198281};
KW Transferase {ECO:0000313|EMBL:SNS44568.1}.
FT DOMAIN 25..232
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 257..391
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 499..738
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
SQ SEQUENCE 889 AA; 95793 MW; F6062970EC422CBB CRC64;
MKTTAPIAID RALAHAPFLR RAAEQRPEIV ERIADQDVAG ALALCAPTDD ADVGRALRRE
RQGLSLAVAL ADLAGLMPFE QVVATLSDFA DRALDRAIAA AIEERTPGEK PQGFAVLGLG
KHGSRELNYS SDIDPILIFD PQTLPRRERD EPIEAAVRIG KRVVELLQHR DAAGYVFRVD
LRLRPSPEAT PIVLPVEAAI SYYESSALPW ERAAFIRARA AAGDIALGEY FLSAIRPFVW
RRALDYGALR EIRSLTRRIR DHHSQGQSFG PGFDLKRGRG GIREIEFFAQ IHQLIHGGRE
PALRAPATLD ALAALAAAGR IDPAEAETLA AAYRLERTIE HRLQMVEDQQ THSLPRQAEA
LDNVAQLHGV ADGAALLDLL RPTVDAVGRI YDGLDEGRAE GLSHDAARVE AALADAGFAD
PASARARIEA WRSGGSRALR SPAAREALEA VLPGLVAALG HAPDANAALN RFDDIVSRLP
SAVPLFRLLE ARPALARMVA DVLVHAPTLA DALGRRPTLL DGLIDASAFN PPPDVPALAA
EIGRREADDD YQMLLDRARQ RVGEKRFALG VQLIERVSDP LDVAAGYARV AEAALVALVD
ATVAEFEAAH GRVPGEGLVI LALGRLGGAA LTHASDLDLI YLFDGDHLAE SDGPKPLGAT
QYYNRLAQRV TAALSVPTAS GPLYEVDTRL RPSGAQGLLA VSMDSFAQYQ RDSAWTWEHM
ALCRARPVYG RPQARAAAAA IIEETLRRPR DPAALLADAV KMRGDMAKHK PPSGPFDVKL
IDGGLVDCEF TVHVQQLRNA TAFDPRLREA IRMLADDGLV SPALGDAYAL LARMLVTFRL
VSPQGGEPLP VSRALVAEAC GQPDWDALLA AYETARATVR AEWARVSAA
//