ID   D4H5T0_DENA2            Unreviewed;       958 AA.
AC   D4H5T0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=(Glutamate--ammonia-ligase) adenylyltransferase {ECO:0000313|EMBL:ADD69521.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:ADD69521.1};
GN   OrderedLocusNames=Dacet_2767 {ECO:0000313|EMBL:ADD69521.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD69521.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD69521.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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DR   EMBL; CP001968; ADD69521.1; -; Genomic_DNA.
DR   RefSeq; WP_013012014.1; NC_013943.1.
DR   AlphaFoldDB; D4H5T0; -.
DR   STRING; 522772.Dacet_2767; -.
DR   PaxDb; 522772-Dacet_2767; -.
DR   KEGG; dap:Dacet_2767; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_1_0; -.
DR   InParanoid; D4H5T0; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000002012; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
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:ADD69521.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ADD69521.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW   Transferase {ECO:0000313|EMBL:ADD69521.1}.
FT   DOMAIN          48..267
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          290..429
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          540..784
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          821..947
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   958 AA;  110408 MW;  4788E84D89331311 CRC64;
     MSSRQDIIRA NASEAGLSER STEALSTVGK HSEFIGVWLV NNIEGLIEAE SKFCGERNRE
     TILNDLLSAD IYAMSPDEFI AYMRRFKMIE YTAIAASDLY FNKSVEEVTA HVSAFASAAC
     QCAYLYSMRE LSEIHGKPVD DDGDEIGFCV VGLGKLGGWE LNFSSDIDII YVYGTDKGKT
     DGADPIETHV FFSRLSEKLT RYIGERTQDG IVFRVDLRLR PDGDRGAICL PVNSYELYYE
     SHGQSWERMM LLKARVVAGD ESVGAGFIER VRPFVFRRSM DFKLLSELKE VKRKINKRVE
     LKGKNIKHVK LGYGGIREIE FVVQTFQILY FPKFPAVFSR NTLKGLDKLR ECGIMDRETV
     IVLSEHYRFL RRLEHMVQIE NERQTHIVPE DSPTYDLYLE RCGFSCDTDF QHAYSEVTQR
     VNDEFAKLFS DDNTTDDNIL AIFDNELTDE DAAHILREIG IKDPIDSVKA VRRIVHGNKN
     RPRLKSDRSV LKVLLPVILR ELKSRDDAYQ ILITFERLLI KASTIYMLHD IFISAPKVLN
     RLINVFSYSS YLTNMILSHI DLLDYVYDPK ETTYDAAEVS SDLWKLTEKY RGDVELELET
     ACIRHRSYIF NIGYAYLNKT INVIDMMRSL TELAKGTVDF AFRTVYEQLL ERYGVPRRKD
     GEECRYLLIG MGKVGSIEMS FGSDIDMVFL FEEQGETDGK KSVTNMEFFS KLVQRANSFL
     NTFTRNGFLY KTDMRLRPSG SSGTLVVSMH GFEDYQKKSA MVWEKQALLR SSVINHYSPL
     LEEFKRIKED VLFTCKLDDD GVQEVYDMRM RIEKEKGLPY EKNNIKAGYG GLLDIEFIAQ
     MLQLKYGCQH SSFRTPNTHD ALHSFRKQGL IKDRDFYSLH KGYLFFRHLE NLVRIYENSD
     TSILPKSDEL RGKIGNFYGF KTDGAVTLMA EYQNIRRAVR AAFNRIFERI SNEDNADS
//