ID   S3Z0R5_9MICO            Unreviewed;       990 AA.
AC   S3Z0R5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1484_01615 {ECO:0000313|EMBL:EPH14315.1};
OS   Dermabacter sp. HFH0086.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH14315.1, ECO:0000313|Proteomes:UP000014577};
RN   [1] {ECO:0000313|EMBL:EPH14315.1, ECO:0000313|Proteomes:UP000014577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HFH0086 {ECO:0000313|EMBL:EPH14315.1,
RC   ECO:0000313|Proteomes:UP000014577};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dermabacter sp. HFH0086.";
RL   Submitted (MAY-2013) 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:EPH14315.1}.
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DR   EMBL; ATFO01000008; EPH14315.1; -; Genomic_DNA.
DR   RefSeq; WP_016664513.1; NZ_KE340308.1.
DR   AlphaFoldDB; S3Z0R5; -.
DR   STRING; 1203568.HMPREF1484_01615; -.
DR   PATRIC; fig|1203568.3.peg.1579; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   Proteomes; UP000014577; 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   Reference proteome {ECO:0000313|Proteomes:UP000014577};
KW   Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT   DOMAIN          97..342
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          372..496
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          602..821
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          846..983
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   990 AA;  109343 MW;  E640EDF305F385B2 CRC64;
     MRLETGAIQA LQAGTGEGEF SHFDLARLGF VRTERSAALL ASDALSRVPP AIVRDMGASA
     DPDEALLALM RLAESAAEAG ESTQFDRVVA DETLGRTLVR ILGSSVALGD ALARHVDALE
     EILECPTLAG PTRERFREVM LAAVGTRADA AVAVAEKGPA PRHAFRRAYY FLLAQIAALD
     VCATDPFAHQ EEISTLLSDL ADAALEGALA LARAATPEHD KVRLAIIAMG KTGARELNYI
     SDVDVMYVAE AARGGVSQEE VTTIGSALAR EVARVCAERT AEGSLWQIDA NLRPEGRDGE
     LVRTLESYAQ YYRKWAHSWE FQALLKARAC AGDTELGAEF ERLTAPLVWQ ASTREGFVED
     TRAMRARVLA RADADRDLKL GRGGLRDIEF TIQLLQMVHG RTDERIREAG TLSALDALTR
     GGYVGREHSV ELADAYRYLR VCEHRLQLWR LRRTHMLPST EPDERRLARG IGTRVENLRA
     DIDAVRRRVR QLHEEIYYRP LLVTSARLSD GQIALSPKEQ RARLEAIGYR DPKRALHHID
     ALTKGLSRAS AIQKQLLPAF LEWFANGVDP DLGLLSFRRL SDTLRETHWF LGMLRDSGAA
     AERLTRILSS SRYVGEQLVL HPYAARWLAN DAQLTPLSRT QLSGELDAIA GRADSEDDVI
     DALRTVRARE IVRISIAHLC GLLDLPSLGE SLTTLAEAIL TFTVEFVQRD TDVELCVVAM
     GSFGAREMGF SSDADVQFVC ARGTEEAIAA ASRVQKILNA PASGINMRVN ADLRPEGRSG
     PLVRTLASFD DYYAHHAERW ESQALLRARV IAGSEDTKAA VTAVMDRARY RAGGMDDRDR
     RDFARMKARI EGERLPRGVK STHHLKLGRG ATTDVEWSVQ RLLLEYAGDD VSLRAVGTLD
     ALAALETAGH LSSADAEALR RAWLLAWELR RALFLWRGRE TDALPTDLVD LRALAALVHE
     PVDNARAIEE RYLKVTRHSR QVAERLIFGE
//