ID A0A433PVZ0_9FUNG Unreviewed; 1252 AA.
AC A0A433PVZ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN ORFNames=BC937DRAFT_91884 {ECO:0000313|EMBL:RUS21677.1};
OS Endogone sp. FLAS-F59071.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Endogonomycetes; Endogonales; Endogonaceae; Endogone.
OX NCBI_TaxID=2340872 {ECO:0000313|EMBL:RUS21677.1, ECO:0000313|Proteomes:UP000278417};
RN [1] {ECO:0000313|EMBL:RUS21677.1, ECO:0000313|Proteomes:UP000278417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FLAS-F59071 {ECO:0000313|EMBL:RUS21677.1,
RC ECO:0000313|Proteomes:UP000278417};
RX PubMed=30485448;
RA Chang Y., Desiro A., Na H., Sandor L., Lipzen A., Clum A., Barry K.,
RA Grigoriev I.V., Martin F.M., Stajich J.E., Smith M.E., Bonito G.,
RA Spatafora J.W.;
RT "Phylogenomics of Endogonaceae and evolution of mycorrhizas within
RT Mucoromycota.";
RL New Phytol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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:RUS21677.1}.
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DR EMBL; RBNK01000445; RUS21677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433PVZ0; -.
DR Proteomes; UP000278417; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR032466; Metal_Hydrolase.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000278417};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 580..1010
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REPEAT 1007..1093
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 1104..1241
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 1252 AA; 136967 MW; 94B37907A02B14AE CRC64;
MAFNPEHNYI AEAIAQIPLL DNHAHNLLEA IATPHDPPLE SCFSEARGAA LADSVNTLPH
SLAVRQLAKL LQCEEDWASV KKARDLLSLE ALSRLCFSRS NIQCILMDDG LASGNERTLP
LEWHDQFLPT STKRIVRVEN VAEGVLATLW DHVLPLKEND VEEVPTDADI AASPPNQKAG
SSLDAEILRN ISTILTQFQT IILHAFGTFA RSNNVAAFKS IAAYRSGLNI SMPLRESVFK
DLHAHYEQYA GSRVVRLTQK ALIDFVVCTA LEVAAEFNLP MQFHAGFGDN DIDLFSANPI
HLKKVIERYP SAKIVILHAA YPYAREAGYL ASVHPNVFVD YGLVHPMVSK GGQRNILKEL
FELTPLNKLL FSTDGHTYPE TFYVAALQAK ESLKEVLLDA IKNEELTIRQ AIEAARNILF
ENANKLYKLK LTPGPINASS HGISFTPAAV HSHLRDLGIQ YIRLTWVDTS NIHRCRVVSV
DRFAAFFREG AAIRGVSLTK AAMALVLNYD AIAPGAGLDA TGEVFLVPDP KTLRKLPYYP
THAICLADMQ EKEVKVVKEE AAKEAAGEVK VVEYEFPLCP RTVLRRVLRQ AKQDLDINFL
IGFETEVIFL REVFPPVAID DTLYGSTASW HANTVGSKIA DEVVDSLAQQ RIKVLQFHSE
SAPGQFEFVT GPLSPLDAVD ALVLTRETIH NVAAKHGVKA TLLPKPFPMS AGTASHVHMS
LKSSSSPAAS TKASSHLPPG LTELEAQFMA GILKHLRALC AFTLPNVNSY ERIAGYYTYI
IFYYSNADIA FHNTSKHQLR LIFLAARSSF TNPCISRRDS EAPLRVAFSP ATTTATRQYN
FELKCLDGTA NPYLAIAAIL SAGLDGVRNG LKVEMQNCKV DPASITAEQR RELGITESIP
KSIHDSLACL KQDALFEKCL GEELLQCFTA VKEAEAKYME DIPEEAIEER RLTKFSVVCV
GSWFKGMTSP VVGVAGLNAI IFASYGGILR AFESRRPPPS SLHSFVPSLS QVYIAGAGAG
LACCLVSTPT EIVKIRAQLT SLPTSGEGSL RAAKEILVKR GLIGFYQGGL VTIIRDVPGY
GVYFYGYEGL KRLLGVTPGS TGGSNTWKLL IAGGTAGVMS WVSIYPIDVI KSRLQAQVLY
PAAPTRSSTQ SPSFHFRSSI TNLQPLTPAP SSTVSKAYHG AIATPSSADA VPPYKGIIDC
AVRSYQAEGL RVFARGIVPT VVRAFPVNSV TFFVYEAIME MLRAVEKQRL SR
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