ID   U1F8K6_9ACTN            Unreviewed;       305 AA.
AC   U1F8K6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glutamate--ammonia ligase {ECO:0000313|EMBL:ERF55803.1};
DE   Flags: Fragment;
GN   ORFNames=H641_07452 {ECO:0000313|EMBL:ERF55803.1};
OS   Cutibacterium granulosum DSM 20700.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF55803.1, ECO:0000313|Proteomes:UP000016307};
RN   [1] {ECO:0000313|EMBL:ERF55803.1, ECO:0000313|Proteomes:UP000016307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF55803.1,
RC   ECO:0000313|Proteomes:UP000016307};
RX   PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA   Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA   Brinkmann V., Meyer T.F., Bruggemann H.;
RT   "Comparative genomics reveals distinct host-interacting traits of three
RT   major human-associated propionibacteria.";
RL   BMC Genomics 14:640-640(2013).
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:PRU01331, 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:ERF55803.1}.
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DR   EMBL; AOSS01000281; ERF55803.1; -; Genomic_DNA.
DR   RefSeq; WP_021104493.1; NZ_AOSS01000281.1.
DR   AlphaFoldDB; U1F8K6; -.
DR   PATRIC; fig|1160719.4.peg.1401; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000016307; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
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   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:ERF55803.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016307}.
FT   DOMAIN          1..305
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ERF55803.1"
SQ   SEQUENCE   305 AA;  33857 MW;  693EF94021ED8721 CRC64;
     HPGDSPEPLD NGGYFDHTTL GAGTDFRRDS ITMLEQMGIS VEFSHHEGAP GQHEIDLRYA
     DALTMADNIM TFRVVIREVA SLKGIKATFM PKPFSQCPGS GMHTHVSLFE GDENAFFDPS
     DEARLSPVAK HFIAGLLHHA PEITAVTNQW VNSYRRIMGG GEAPAYICWG RNNRSALVRV
     PAYKPNKASS ARVEVRSVDA ATNPYLALAL ILAAGLSGIE HEWELPEEAS DDVWSLSARE
     RRALGIDPLP KHLGQAIALM EDSELVAETL GEHVFDYFLR NKKAEYEEYL GQVTQFELDR
     YLPHL
//