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Database: UniProt
Entry: F3Z283_DESAF
LinkDB: F3Z283_DESAF
Original site: F3Z283_DESAF 
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
//
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