ID F3Z283_DESAF Unreviewed; 715 AA.
AC F3Z283;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:EGJ50123.1};
GN ORFNames=Desaf_1788 {ECO:0000313|EMBL:EGJ50123.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ50123.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ50123.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ50123.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP003221; EGJ50123.1; -; Genomic_DNA.
DR RefSeq; WP_014259883.1; NC_016629.1.
DR AlphaFoldDB; F3Z283; -.
DR STRING; 690850.Desaf_1788; -.
DR KEGG; daf:Desaf_1788; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1560; -; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR040577; Gln-synt_C.
DR InterPro; IPR008147; Gln_synt_N.
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 InterPro; IPR022147; GSIII_N.
DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF18318; Gln-synt_C-ter; 1.
DR Pfam; PF12437; GSIII_N; 1.
DR SMART; SM01230; Gln-synt_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000007844}.
FT DOMAIN 89..182
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 187..622
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 715 AA; 78714 MW; 89E9720532512826 CRC64;
MSGSQARVKA IAAITKYKAE KPGKPVEGLK LEKLYGANVF SESVMQERLP KAIFKSLKKT
IKTGAKLDPT VADAVATAMK DWAISKGATH YTHVFYPLTG LTAEKHDSFL VPDGKGGAMA
EFEGKQLIQG EPDASSFPSG GLRSTFEARG YTAWDVTSPA YIMESPNGTT LCIPTAFLSW
TGEALDKKTP LLRSLQALDK QARRVLKLFG KEPKDRVTCF AGIEQEYFLI DRNFFFARPD
LFIAGRSLFG CKPPKGQEFE DQYFGAIPRR VLNCMMEVEE DLYKMGIPVK TRHNEVAPSQ
YEIAPLFEEG NTATDHNHLV MHTLRRVAKR YGLACLLHEK PFAGINGSGK HLNYSIGNSE
LGSLFDPGDT PHENMQFLVF CAAAIRAVHK YGAVLRSTVA SASNDHRLGA NEAPPAIMSM
YLGEMLTDVF TQIKNGGAKS SKAKSVMNIG VDTLPPLPMD PGDRNRTSPF AFTGNRFEFR
AVGSSMSVAG PQVALNAMMT ESLDFIATEL EKKTGGDTKK LSKAVQEVLQ EIMQKHDAII
FNGDGYSEAW HKEAEKRGLP NLRCTPEALP ALTTPETLDL FTKYGIFSER ELRSRQDIYV
EYYCRTVMSE ANLVVKMAKT TIYPAALQYQ KDLAGTGSAL EKPVKDKAAA LLDAVARLEK
AMAMHLPDIL EEAKHLCGVV LPAMNDVRAV ADDLEGLVAD DLWPLPSYME MLFIK
//