ID S3XU85_9MICO Unreviewed; 436 AA.
AC S3XU85;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Glutamine synthetase, type I {ECO:0000313|EMBL:EPH14314.1};
GN ORFNames=HMPREF1484_01614 {ECO:0000313|EMBL:EPH14314.1};
OS Dermabacter sp. HFH0086.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Dermabacter.
OX NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH14314.1, ECO:0000313|Proteomes:UP000014577};
RN [1] {ECO:0000313|EMBL:EPH14314.1, ECO:0000313|Proteomes:UP000014577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HFH0086 {ECO:0000313|EMBL:EPH14314.1,
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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:EPH14314.1}.
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DR EMBL; ATFO01000008; EPH14314.1; -; Genomic_DNA.
DR AlphaFoldDB; S3XU85; -.
DR STRING; 1203568.HMPREF1484_01614; -.
DR PATRIC; fig|1203568.3.peg.1578; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_3_11; -.
DR Proteomes; UP000014577; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF11; GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000014577}.
FT DOMAIN 8..92
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 99..436
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 436 AA; 49253 MW; 3BFA78E4C3F755DF CRC64;
MLRQVEEQGI DYIRLWFSDV VGRLKSIVIS PHDLDKAFDE GIGIDGSAIE GLTRSYESDM
LLRPDPSTFR VMGAPRGGEA GVMICDVFTP DSEPAASDPR RVLRDALARA EAKGLEFFTH
PEVEFYLFER AYEQGVGLTP VDQGGYFDYV QRVDGSRFRR DAMRELERMN IHVEYSHHEG
GPGQNEIDLR YADALTTADN LLTLRAVVKG IALSEGKFAS FMPKPMIEHP GNGMHTHLSL
FQNGTNIFHE PGAEYGLSRT ARHFIAGLLV HAREYSILTN QFVNSYKRLW GEQEAPSYIV
WGHNNRSALV RVPFHKPTKG TSSRVEFRGL DSAANPYLAF AALLAAGLKG IEEEYPLPEG
AEDTVWELTE RERNAMGIEP LPSDLLRAIE SFETSELMAD VLGEQVFEYI LRDKRREWEG
YRRQVTDSEL RTTFDI
//
