GenomeNet

Database: UniProt
Entry: S3XAX9_9ACTN
LinkDB: S3XAX9_9ACTN
Original site: S3XAX9_9ACTN 
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
//
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