ID B2URJ8_AKKM8 Unreviewed; 703 AA.
AC B2URJ8;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:ACD05083.1};
GN OrderedLocusNames=Amuc_1258 {ECO:0000313|EMBL:ACD05083.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05083.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(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; CP001071; ACD05083.1; -; Genomic_DNA.
DR RefSeq; WP_012420298.1; NZ_CP071807.1.
DR AlphaFoldDB; B2URJ8; -.
DR STRING; 349741.Amuc_1258; -.
DR PaxDb; 349741-Amuc_1258; -.
DR KEGG; amu:Amuc_1258; -.
DR eggNOG; COG3968; Bacteria.
DR HOGENOM; CLU_024307_0_0_0; -.
DR OrthoDB; 9807095at2; -.
DR BioCyc; AMUC349741:G1GBX-1344-MONOMER; -.
DR Proteomes; UP000001031; 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:UP000001031}.
FT DOMAIN 74..167
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 179..606
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 703 AA; 77928 MW; 46020EFCB4B36C65 CRC64;
MHTNPPSDVG NAATFIAEIY GQDVFNMETM RNYLPRPVYK KLLATIRKDE KLDPDIANEV
AQAMMTWALE KGASHYTHWF QPLNGSTAEK HDSFVDVDPE GNLELKFSGK SLVQGEPDAS
SFPSGGLRAT FEARGYTAWD PTSPAFIKRT ENGATLCIPT AFCSYKGQAL DKKTPLLRSM
TAVTRQAKRL LSCFGGPDNI HVSADLGAEQ EYFLVDKQLY ALRPDLMMCG RTLFGNVPPK
HQQMEDHYFG SIKDRVLEFM VDVDEALWKL GIPAKTRHNE VAPGQFEIAP IFESQNLAVD
HNMLVMEVLR KTANKHDMVC LLHEKPFSGM NGSGKHNNWS LSAPGYGSLL NPGSSPQENA
IFLTLLCATI KAVDEHADLL RASVAKSGNE HRLGAHEAPP AIISIFLGDL LDEIIEQIEK
GGTKKARTQK TINIGVDTLP MFPLDASDRN RTSPFAFTGN KFEFRAVGSS QTCAWPMTVL
NTIVAESLDE ICTILEPVKD KPEEFHATLN KLLQNIIKKH KRILFSGDGY GEAWVEEAER
RNLPNIPGTI EALAALETPK AKALFEKYKV VSPVELHARH EIQTEIFHKE INIEAETALL
MVETLYIPAV TEQLTQLTTA IAQMKASGIK AGMKATTDRA NQIGTLLDIL PGQVRELRRA
VDEADTRAIQ TGMDNLRSTI DMLESLTDAD LWPVPTYAEL LFL
//
