ID S3XAX9_9ACTN Unreviewed; 984 AA.
AC S3XAX9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=[glutamate-ammonia-ligase] adenylyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1531_01841 {ECO:0000313|EMBL:EPH02533.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02533.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH02533.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02533.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
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:EPH02533.1}.
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DR EMBL; ATFL01000014; EPH02533.1; -; Genomic_DNA.
DR RefSeq; WP_016669629.1; NZ_KE340297.1.
DR AlphaFoldDB; S3XAX9; -.
DR STRING; 1203605.HMPREF1531_01841; -.
DR PATRIC; fig|1203605.3.peg.1901; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000014567; 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:UP000014567};
KW Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT DOMAIN 113..323
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 346..482
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 588..817
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 839..978
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 984 AA; 107518 MW; 431CF234F99CD378 CRC64;
MGGRTNSMVG ELARLGFSDV TRSATRVAEL ESTLASEAPG WLEVVASVPG PDLALQQLSA
INYDDPGMVQ AIFADEIWAH RLVSVLGASQ GLGLHLRAHP GDAEVIRGDL NAFDRAGIWA
RMAECIGADL EQDSPMGIIK DPAAADLLRL ANRRELLRIA ARDLTHPEPI KILDEICAEL
SDLADAVLQF ALAIARAQTP GHDKVRLGIL AMGKCGAQEI NYLSDVDVVH VAEPVEGVGV
EEAMQIGARL AGALARICSA HSAAGTIWQV DAALRPEGKA GPLVRTLESH RVYYEKFAKN
WEFQAMLKTR PAAGDLELGQ QFCEMIDPMV WQVGGAPNFM ADTQAMRKRV VSLIPATEKK
REIKLGAGGL RDVEFSVQML QLVHGRVDAS VRTRGTLESL HALMAGGYIG RADGKRLDEA
YRFLRVLEHR EQLARLRRTH LMPDNDVDQR RLARQIGCAD AEELMTAWHS TTREVLALQQ
RIFYSPLLEA VSRLSGEELR MSPQAATDRL HAMGFADPAA ALRHMEALTT GLSRTAQIQR
QLMPAMLRWF SEGPNPDLGL LTFRRLSEAM GATSWYMRAL RDEDWMAERL AKIASSSRYV
SEILRKDPSV VQLLASEEST TPRGRQELAE SMAKVIDRHG SDHEAAVHAI RSLRTRELFR
LAAGDILEVT DLATLGQGLS DLASASVDAI LEVAARAVEG PRTRIGVVAM GRWGGNELGY
ASDADVMYVV DDQAGPGQIA WATQVITRAK SWLGTPGVAR LVMDAGLRPD GKSGPLVRSL
GSFCSYYEKW ADTWEFQALL RAGHGAGDRD LTEALLEAIE AVRYPPEGID DKQVAEIRRL
KARMETERTK GKAAGNLKLG LGGLSDVEWT AQLIQLRHAG AHPGLRTTRT VPVLITARDL
GLINASDADA LIEAWTTASK LRNKTMLVRG RSSDQLPVDP REIASVSLLL GYEPGHASEL
LQDWAKQARY ANQVVDRLFW GAQG
//