ID D9UHZ5_STRS3 Unreviewed; 1009 AA.
AC D9UHZ5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:EFK99371.1};
GN ORFNames=SSLG_01430 {ECO:0000313|EMBL:EFK99371.1};
OS Streptomyces sp. (strain SPB78).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591157 {ECO:0000313|EMBL:EFK99371.1, ECO:0000313|Proteomes:UP000005781};
RN [1] {ECO:0000313|EMBL:EFK99371.1, ECO:0000313|Proteomes:UP000005781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB78 {ECO:0000313|EMBL:EFK99371.1,
RC ECO:0000313|Proteomes:UP000005781};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain SPB78.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657742; EFK99371.1; -; Genomic_DNA.
DR AlphaFoldDB; D9UHZ5; -.
DR STRING; 591157.SSLG_01430; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR Proteomes; UP000005781; 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; 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 Ligase {ECO:0000313|EMBL:EFK99371.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EFK99371.1}; Transferase {ECO:0000313|EMBL:EFK99371.1}.
FT DOMAIN 203..324
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 359..488
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 593..839
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 865..1004
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 29..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..93
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 111138 MW; F70565774ACB3654 CRC64;
MMAGGRGDDR PERAQEQYLH AAAAVRVRRS LARGEAARRG RPRGRALRPR AARRARGRGR
PGSRAARTRP ARRGAARRRG AAHPAHHARL PRSRLRDRLL GVLGRLPRPS PTTSRATRAT
GRPWSRTSRA TCTPMSAEFE RGLADVTNPV SLASPTRLPP VARRPRRHGH HRRQRDRRRT
RRPRNRERCG TALRLAQEAA PEDAAACRLA VIAMGKCGGH ELNYVSDVDV IYVSEPAHDG
VDEGEAIRAA TRLAAHLMRI CSETTVEGTI WPVDANLRPE GRNGPLVRTL SSHLAYYHRW
AKTWEFQALL KARPVAGDLA LGQEYVEALA PLVWQASERE NFVTDTQRMR RRVIDAIPAA
EAERELKLGP GGLRDVEFAV QLLQLVHGRT DTNLRSPTTL AALAELADGG YIGRTDAFQL
DEAYRFLRSL EHRIQLFKLR RTHLVPEDEA DLRRLGRSLG LRTEPIASLL KEWKRHSGAA
RRIHEKLFYR PLLDAVAHLA PGEAGLSPAA ARDRLVALGY ADPAAALRHL EALTNGVSRR
AAIQRTLLPV LLAWFADSAD PDAGLLNFRK VSDALGKTPW YLRLLRDEGA AAENLARVLS
AGRLAPDLLL RAPEAVALLG DPAGLDPRPR AQLEQEILAA VGRAETPEAG VVAARGVRRR
ELFRTAAADL IGSYGTEDTP AEEDHGALVD RVGSAVSDLT AATLAGTLRA VVRAGWGEEL
PTRFAVIGMG RFGGHELAYG SDADVLFVHA PREGVDEAEA ARAANAVVAE MRRLLQLPSA
DPPLLIDTDL RPEGRNGPLV RTVSSYAAYY RRWSQTWEAQ ALLRAEPVAG DTGLGRAFTE
LIDPLRYPAE GIGEEAVREI RRLKARMEAE RVPRGQDPNL HTKLGRGGLS DVEWTVQLLQ
LRHGHHEPGL RTTRTREALA AAFEADLLDQ EQARILDEAW VLAARVRNAV MLVRGRAGDT
FPSDTRELGA VSRYLGYEAG HAGDMLEDYR RTTRRARGVV EELFYGAAL
//
