ID A0A1F1KHB5_9MICO Unreviewed; 901 AA.
AC A0A1F1KHB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:OFS14962.1};
DE Flags: Fragment;
GN ORFNames=HMPREF3099_03070 {ECO:0000313|EMBL:OFS14962.1};
OS Kytococcus sp. HMSC28H12.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=1581067 {ECO:0000313|EMBL:OFS14962.1, ECO:0000313|Proteomes:UP000176675};
RN [1] {ECO:0000313|EMBL:OFS14962.1, ECO:0000313|Proteomes:UP000176675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28H12 {ECO:0000313|EMBL:OFS14962.1,
RC ECO:0000313|Proteomes:UP000176675};
RA Ploux O.;
RL Submitted (MAR-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:OFS14962.1}.
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DR EMBL; LWPN01000088; OFS14962.1; -; Genomic_DNA.
DR RefSeq; WP_070703839.1; NZ_KV824336.1.
DR AlphaFoldDB; A0A1F1KHB5; -.
DR Proteomes; UP000176675; 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:OFS14962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000176675};
KW Transferase {ECO:0000313|EMBL:OFS14962.1}.
FT DOMAIN 11..244
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 267..407
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 512..732
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 774..899
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OFS14962.1"
SQ SEQUENCE 901 AA; 96985 MW; FA241E8ABF8ADFED CRC64;
AGPDAERGPL ARLVAVLGAS QVLGDHLARH PEHLELLDAE TLPTPEEARE VLVAAVSEAV
AAGESGDDAL RVAYRGQLVR VAGLDLTAPD PTEVVDAVAA ALADLAAGAL EAALVIARHE
VDHAEDVRLA VIGMGKTGGR ELNYVSDVDV IFAAEPAEGV EEARALQVGA RLATRLVQAC
GATTAEGTLW PVDAALRPEG KAGPLVRTLE SFRGYYERWA STWEFQALLK ARPVAGDPEL
GQAFVDLVDP MVWQVATRDG FVEGVQAMRR RVEAHIPAAE AKRQLKLGAG GLRDIEFSVQ
LLQLVHGRVD ESLRSGSTLP GLTALAAGGY VARSDAAVLD PAYRLLRALE HRIQLDRLRR
SHLLPVDEDD LRRLGRAMGW TKDPAQEVER RWAEVSKEVR RLHERLFYRP VLSALSDLTP
TQARMSPDAV TERLAALGFA DPAGSVRHLE SLTRGVSRTA AIQRQLLPAM LGWFAGWPAP
DAGLLAFRRI SESLGGTHWY MAMLRDEGHA AQRFAHVLSA SRYLTGLLER GPDAVRLLGE
PDALVPPSRE AVVSRMRSAV GRAGSVEDAA TAARVLRRTE VLRLGIGRLT GQVDSAQVQE
GLTNAAEALL DAVLEAALDG DSTGVAVIGM GRLGGGEMGF ASDADVFLVH DDAPGRAEAA
TAALKALRST LVAGSEPPLE VDIDLRPEGR SGPTVRGIAS LEQYYERWSS PWEAQALVRA
RPVAGDAELC ARVMVLVDPR RYPEGGLTPA ALREMRVLKA RMEAERIPRG GDPRLHLKLG
RGGLSDVEWT VQMLQMEHAA RLADLRTAST RQALTALRGH ELLSAADAEA LSEAWEMAGE
VRDASMLWRG RASDSIPTDP LDREGVSRAM GRPAGAGAEL TEEYLRRSRR ARAVVERVFF
A
//
