ID U7D8R1_9BACT Unreviewed; 729 AA.
AC U7D8R1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:ERP31482.1};
GN ORFNames=CALK_1526 {ECO:0000313|EMBL:ERP31482.1};
OS Chitinivibrio alkaliphilus ACht1.
OC Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC Chitinivibrionaceae; Chitinivibrio.
OX NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP31482.1, ECO:0000313|Proteomes:UP000017148};
RN [1] {ECO:0000313|EMBL:ERP31482.1, ECO:0000313|Proteomes:UP000017148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACht1 {ECO:0000313|EMBL:ERP31482.1,
RC ECO:0000313|Proteomes:UP000017148};
RX PubMed=24112708;
RA Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA Muyzer G., Mardanov A.V., Ravin N.V.;
RT "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT candidate phylum Termite Group 3.";
RL Environ. Microbiol. 0:0-0(2013).
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:ERP31482.1}.
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DR EMBL; ASJR01000012; ERP31482.1; -; Genomic_DNA.
DR AlphaFoldDB; U7D8R1; -.
DR STRING; 1313304.CALK_1526; -.
DR PATRIC; fig|1313304.3.peg.1458; -.
DR eggNOG; COG3968; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000017148; 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; 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:UP000017148}.
FT DOMAIN 83..176
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 188..612
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 729 AA; 82116 MW; 6A2E8CF3DECC47F1 CRC64;
MSNRREVAAH IDKSRPGHVR EVERVSTYYG SNTFSEDKMR KRVPEKVFTA FKEWQNGGEQ
ICSAFADQIA QAMMEWALEK GATSYTHWFQ PMTGLTAEKH DSFISRNGKA QVIEQFSGKN
LILSEPDASS LPSGGLRTTF EARGYTAWDP SSPAFIREVE FGKTLCIPSI FVSYNGEALD
KKLPLLRSEK AVTQAAERLL RIFSKDDVSV KTTCGAEQEF FLIDEGYYRL RPDLQLTGRT
LLGAPSAKGQ QLEDQYFGSI KDRVLNFMND VEKEAYKLGI PITTRHNEVA PSQFEFAPIF
EDSALAADHN QLLMDILKKI ARKHRLVCLL HEKPFAGVNG SGKHINWSLA DSRGGNLLNP
GSTPHDNIQF LTLLTGIISA VYTHGDILRA SVASAGNTHR LGANEAPPAI MSIFLGSQLS
NIVDAIVNGR PVGADDDNRM STGISFIPDI ERDQTDRNRT SPFAFTGAKF EFRAVGSEMN
ISTPLMVINT IVAEGFDALS DALEAAGENL SVTAITAVLQ KFLQESKDIL FEGDNYSREW
EEEAARRNLP NVVSTAKALE AYISKKTISL FERYEVLNSS ELHARYMIWL ELYNNLLVIE
AETLEELVQT EVLPTAYKFQ REVGESLRVL RDMDQDDSIP LPIHAVEDRI EMFAHITEDI
YIVRKHIHKL RDMLKIISKK SDQAERADYL TNDLTPHFEH IRKHVDHLES TIADDLWELP
KYREMLFNL
//
