ID E8TN76_MESCW Unreviewed; 440 AA.
AC E8TN76;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:ADV11634.1};
GN OrderedLocusNames=Mesci_2489 {ECO:0000313|EMBL:ADV11634.1};
OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS WSM1271).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV11634.1, ECO:0000313|Proteomes:UP000007471};
RN [1] {ECO:0000313|Proteomes:UP000007471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC {ECO:0000313|Proteomes:UP000007471};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA Tiwari R.P., Woyke T.;
RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT WSM1271.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
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}.
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DR EMBL; CP002447; ADV11634.1; -; Genomic_DNA.
DR RefSeq; WP_013530317.1; NC_014923.1.
DR RefSeq; YP_004141684.1; NC_014923.1.
DR AlphaFoldDB; E8TN76; -.
DR STRING; 765698.Mesci_2489; -.
DR KEGG; mci:Mesci_2489; -.
DR PATRIC; fig|765698.3.peg.2966; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_6_0_5; -.
DR OrthoDB; 9789509at2; -.
DR Proteomes; UP000007471; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF16952; Gln-synt_N_2; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231}.
FT DOMAIN 105..440
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 440 AA; 46763 MW; 0E99FD2658BD707B CRC64;
MTSTVEPLVA VVTTDLSAVT RGRFVAESKL QKTATTGVGW LQANLSLTPF NSIVDPNPWG
SSGDLRLIPD LEARFRTTRT GSATPFDMVA GDIVELDGSP WLGCTRTMLK DALADLKAAT
GLSVIAAFEH EFNVADGGFA QAHSMSFAAL RRADPFAPNL MAALEEAGVA PEVVIAEFGD
EQFEVTHEPA DALTAADRAV AIREITRELA RNAGWRASFA PKTAPTAVGN GVHIHFSFVD
EAGKPMTYDP ALAGGLSAKA GAFCAGVLRH LPGMTAMTAS SVSSFYRLKP HSWSSSYTWL
ADRDREASLR ICPTVTIGGR DPARQYNIEY RAADATGNPY LSLAAIIRAG LEGLEAGLPS
PPLVTGDPTL MSEAERASLG LVRLPETLPA ALDALLADGT VTGWFAPVFI ETFVGLKRHE
AERLAGLDPA SICDLYRTLY
//
