ID A0A1B7LZB2_9MICC Unreviewed; 1026 AA.
AC A0A1B7LZB2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:OAV60854.1};
GN ORFNames=A6F49_10220 {ECO:0000313|EMBL:OAV60854.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV60854.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV60854.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV60854.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-2016) 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:OAV60854.1}.
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DR EMBL; LXEY01000018; OAV60854.1; -; Genomic_DNA.
DR RefSeq; WP_043057892.1; NZ_LXEY01000018.1.
DR AlphaFoldDB; A0A1B7LZB2; -.
DR STRING; 1837282.A6F49_10220; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000078292; 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:OAV60854.1}; Transferase {ECO:0000313|EMBL:OAV60854.1}.
FT DOMAIN 77..340
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 362..506
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 611..853
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 875..1017
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 1026 AA; 114126 MW; 67252E824F1E2855 CRC64;
MSQPLSQRTL LSAGLQDTTR AESLLQSKEL AGLDLEDLLR QLAVAPDSDT ALLLLIRLIE
RDPTVAQLVT DDAARPLLRL LGASEALGEY LIRRPEHLDI FRNPQVESTP ASGGLVDAHG
HRVDGAEMLR ARLLESVGAD PHDPTPIATI TGKDASVALR IAYRRQLVAI AVEDLIAEDP
VEMQPVVSVW LSDLATAALE AALAVSRAET LTRHNDANDV ELTVIAMGKC GARELNYFSD
VDVIFAHDVL EGSQLTRQDA TDIAVELAAG ISTVVNQPAR EPALWEVDTN LRPEGQDGAL
SRTISSHLEY YQRWAHTWEF QALLKARPVA GSLELGQRYL DTLHPLIWQA STREGFVRQV
QRMRHRVIDH ISHDQRQREI KLGPGGLRDV EFPAQLLQLV HGKTDPELRV RATEDALEAL
QAGSYIGPSD AQVMTNNYRF LRLIEHRVQL VQLRRTHMMP DTEPELRMLT RSVRPMGGKW
PKDHEQLVKA WQATVRSNRT LFEQIFYRPL LPSTAALSPD DARLTPEAAT ARLAALGYRD
PQGAVRHIES LTSGVSRQAK LQRQILPAML GWLASGPDPD GGLLGFRKLS ESVGGSHWYL
HMLRDSSAAG ERLAHVLSSS RYIADMLEHT PQAAAWMDRD QDLMPLSLET IQTEMTALIQ
RHPNLPDAAR YVRVVRRREI LRISLADACD LVEQQQVSEA LAAADQAAVE ALLQLVQDHV
TEKWGGAGPR AEVAVIAMGR QGGYEAGYGS DLDVMFVHQP AQDVAVDEAS RFAVDVAKAL
MSFMKMPMRP PIVLEPVLEI DADLRPEGRR GPLVRSLDSY RAYYEQWADT WEIQALLKAR
AIAGPLHLQD AFTQWADSVR YTHGLNDSQA QEIRRMKARV EAERLPRGAD PARHLKLGRG
GLTDVEWLTQ TLQLRHAPEH AQLRTTNTLE ALEAARAAQL VTTQDAEILI HAWSFATRIR
SGIVISTGKV SDVLPTNREQ LEALARWTGY DAGEVGEFED DYLRITRHAR AVFERIFYGT
PSPRTV
//
