ID D4YNY6_9MICO Unreviewed; 996 AA.
AC D4YNY6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=[glutamate--ammonia-ligase] adenylyltransferase {ECO:0000313|EMBL:EFG47126.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:EFG47126.1};
GN Name=glnE {ECO:0000313|EMBL:EFG47126.1};
GN ORFNames=HMPREF0183_1646 {ECO:0000313|EMBL:EFG47126.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47126.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG47126.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47126.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) 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:EFG47126.1}.
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DR EMBL; ADNU01000046; EFG47126.1; -; Genomic_DNA.
DR RefSeq; WP_005884831.1; NZ_ADNU01000046.1.
DR AlphaFoldDB; D4YNY6; -.
DR STRING; 585530.HMPREF0183_1646; -.
DR eggNOG; COG1391; Bacteria.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000005714; 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; 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:EFG47126.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:EFG47126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005714};
KW Transferase {ECO:0000313|EMBL:EFG47126.1}.
FT DOMAIN 79..322
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 357..485
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 589..825
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 848..987
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 996 AA; 111036 MW; D78FDAADA648EC12 CRC64;
MRKKDPARHR SQALERTQRF LGQFDEMLGT QLAQDPESAL AAAADRDSAA LGLVRIAEAC
QQNDINLRQL LDESPILLNR LIIVSGGSEA TVDHLVRWPQ FIRTLAHEPD FIDSLASTPE
ALEDTFTEAL ADKGSLLTGD EGITALRRTY RDLVTRLVVQ DLEHAQPEEI VEDVTRVLSD
LAAAVFQAAY KIAEVEQGER LRARIAVVAM GKCGARELNY VSDVDVIFAY APREGEELDD
EVREQATHLA TRVTELISGG AHEPALWEID TALRPEGKSG ALVRTIDEFV QYYQKVAHNW
EFQALLKARP IAGCPELCEQ FEDDVSPFVW TAGARSGFVS EVRSMRRRVV SLIPKNELDR
HIKLGPGGLR DVEFTVQLLQ LVHGPHDEDL RVRSTGGALR ILSSHNYLAS HEARTLASAY
RFMRVVEHRL QIPRMAREAV LPERASKLRA LARSVYPVEE RSVDRLKKEL AGHMRAVRAL
HKQIFYRPIL DAATGSAQMS TVSEAVARDR LTAFGYQDPA AAMRHIRALS TGLNRVAYVQ
RQVLPALLDW FSRGVDPDAG LVAFRRLSEG LSHTTWYLAM LRDSGVAVKN MARVLSLSRF
ASDLLISHPQ SVQWLGNNER LQPSEPDAIA TRMRERSRRR DDGVAAIRKV YGEEILRTSL
ADTLGLYDLD TVMTALTNAM DITVHQALSH VRMRLDAMSG IDDYRFCIIA MGRLGGAEIG
YYSDADVMFV YEPGETLTPA QREALPSHAK QVALTLTSEL ETRSAEPIVD IDADLRPEGK
SGPLVRTLSS YAKYYAAWSE PWEAQALLRA RPIAGDEELG QAFTRLIDPL RYPEEVPESS
LMQMRRLKAR MESERLPRGG DKKRHLKLGT GGLSDVEWTV QMLQLQHAHT HPGLRTTSTL
DALHAATQNG LIDEDSAHKL EAAWTIASRV RSAAVLYKGR GSDSLPTDET ELEAIALLLG
YEPGGGYQLV DDYLGATRRA RKVMEHVFFG FEPEDI
//
