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Database: UniProt
Entry: K5YZ20_9PROT
LinkDB: K5YZ20_9PROT
Original site: K5YZ20_9PROT 
ID   K5YZ20_9PROT            Unreviewed;       948 AA.
AC   K5YZ20;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:EKN00204.1};
GN   ORFNames=MXAZACID_06576 {ECO:0000313|EMBL:EKN00204.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKN00204.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKN00204.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKN00204.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
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:EKN00204.1}.
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DR   EMBL; AMPS01000081; EKN00204.1; -; Genomic_DNA.
DR   RefSeq; WP_008493415.1; NZ_JH976207.1.
DR   AlphaFoldDB; K5YZ20; -.
DR   STRING; 1214225.MXAZACID_06576; -.
DR   PATRIC; fig|1214225.3.peg.1274; -.
DR   HOGENOM; CLU_006233_0_0_5; -.
DR   Proteomes; UP000006217; 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   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 1.
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:EKN00204.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:EKN00204.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   Transferase {ECO:0000313|EMBL:EKN00204.1}.
FT   DOMAIN          46..287
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          308..443
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          555..784
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          824..889
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   948 AA;  101251 MW;  49CC4B6EBCE01F40 CRC64;
     MPGDLHKPSF PKPADQAAAA RLRADFAALG PREAKLARSD SGAALLAALG GNAPFLAELA
     CRESATLCAC LEAGPTPQAK AVLAGLASLP PDLPRAQLSD ALRRAKRQMA LSIAIADLGG
     LWTLEQVTAA LSDLAETALR AAIRHLLYEL HAAEEIALPD PAAPDQGSGF VALALGKLGA
     RELNYSSDID LVLLYDPESP VYGEDSQPMM ARLARDLTAL LAARDAEGYV FRVDLRLRPD
     PGATPPVVAL ATALSYYESH GRTWERAAFS KARPVAGDLA LGQQFLAAIR PFIWRKYLDF
     AAISDIHEMK RQIDAQHPAE GLRGFDVKLG QGGIREIEFI VQTLGLVWGG QDPALRIPAT
     LEALPAMARA GHLPERAARQ LAADYRELRR VEHRLQMVAD RQTHALPASE AGLEAFCIFL
     AAPRFRQSFP KLLARVHAHF LDFFDAGTQA LQDGLNPGPE GAPAPAFTAR LEALGFKDIK
     HIAARLRDWG SGDMPALRSP RARELLDGLV APLLAALGAQ PEPDKAFAQF DTLLSRQRAG
     VQLLSLFTRN PGLLKRLAAV LGAAPALSDY LTEDPQALDG LLAPEARFAA PRPVLRRLLA
     EAEDLEQAAA ATRRFVRQEE FHLSVATLEG RLDANEAGRT RSALAEAALS QLLPLVIAAQ
     KQRQPAPRGA KVAVLALGKA GAGEMLAGSD LDLMLIYDHA PMAIPPTQWF SRLSQAFVAA
     LTAQGPGGPV YHVDMRLRPS GNAGPVAVSL ASFRSYHAKE SWTWERLALT RARVMAATPG
     FAATVREAVL GALCRPEPRA RILADTAAMQ ARLAAEMKPR GPFDVRAIPG GMMEVGFIAQ
     ALQLIHGGSE PALFQPNTEA ALKGLAAAGL LRQSDAEALI AADRLWRTIQ GINRITGLPL
     SAAAPPGAML EPLLRATFFA DLAALQAGMR EAAAQAHQIF TQTFTEGA
//
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