ID A0A1S9ZPE3_9GAMM Unreviewed; 1487 AA.
AC A0A1S9ZPE3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OOR85243.1};
GN ORFNames=B0180_00125 {ECO:0000313|EMBL:OOR85243.1};
OS Moraxella canis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR85243.1, ECO:0000313|Proteomes:UP000190322};
RN [1] {ECO:0000313|EMBL:OOR85243.1, ECO:0000313|Proteomes:UP000190322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR85243.1,
RC ECO:0000313|Proteomes:UP000190322};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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:OOR85243.1}.
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DR EMBL; MUXT01000001; OOR85243.1; -; Genomic_DNA.
DR Proteomes; UP000190322; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 20..410
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1487 AA; 162070 MW; A206FF61D0E9578C CRC64;
MTMISSTTYL ASPDDFSDNC GFGLIAHVEG TPSHDLVKTA IHSLSCMTHR GGVAADGRTG
DGCGLLIAKP DAFFRAVAAE NGFELSENFA VGTVFVNLDQ AKAKHSMQVL NEAITGEGLE
VAGWRDVPVN LDIVGDIARE SLPDFKQVFV NAPKDMPADE FNRLLFVARK KAELQLTEDE
LFYVTALNCQ TVIYKGLVMP KDLPNFFLDL QDDRLSSHIV VFHQRFSTNT LPRWNLAQPF
RYLAHNGELN TITGNRNWSV ARTPKLKSDK LPELQALAPL VNSTGSDSSS LDNMLEVLMN
GGMSLFHAMS ILVPPAWQNV DSMDMDLRAF YEFYSPHMEA WDGPAGLVIQ DGRYAVCMLD
RNGLRPSRWV TTKNGYITVA SEVGTWDYTP DDVLAKGRIG PGQMLVIDTY SGQIMDTKTI
ATILKKAHPY RKWLRENAMR IRDNQAIELS LASATKDTEH LAALQKMFHI TSEERTEIIR
PAAENAQEAV GSMGDDTPMA VLSRQIRHVA DFFRQQFAQV TNPPIDPLRE SIVMSLQTCL
GAQTDVFNPT SKDAHRIILS SPILSASKMQ QIEATQDPAF LSQRIDLNYD DSLSLKQAID
NICQEVVAAI KQGYTLIILS DKNIKKGKVP ANAVLVTGAV HHHLIQQGLR ADANLIIETG
LVRDPHHAAV LIGFGATCIY PYLTYEVIDH LVETGEINTD ALSARANFRK SLDKGLLKIL
SKMGISTIVS YRGAQLFEAV GLSPEIVDLC FVGVASRIKG ATFEDLANDQ AILAKNAFTR
RTPLDKGGLI KFVFDKEYHA FNPDVVRALH SAVRSGDYQE YQKYADIVNH RPVATIRDLL
ALKTGSEIDL DEVEGIESIL PRFDSAGMSL GALSPEAHES IAMAMNTIGG RSNSGEGGED
PARYGTLKNS KIKQIASGRF GVTPAYLRSA EVLQIKIAQG AKPGEGGQLP GGKVNDLIAR
LRYSVPGVTL ISPPPHHDIY SIEDLAQLIF DLKQVNPSAL VSVKLVSRPG VGTIATGVAK
AYADLITISG YDGGTAASPL SSIHYAGSPW ELGLAEAHQS LRVNGLRDKV RIQTDGGLKT
GLDVVKAAIL GAESFGFGTA PMLAVGCKYL RICHLNNCPT GVATQRIDLR DEHYIGEVDM
LINFFKFVAM ETRHWMAKLG VRTLEELVGR TDLLDILEGQ TPKQQHLDLT PLLYSHPRAA
DAPHTCQVPS NVPFDQGILA ERMVSDMAIS IKKGYGGEYS YRISNCDRSI GARISGEIAD
TWGNLGMSDK PIKLHLTGTA GQSLGVWNAG GLNIELEGDA NDYVGKGMAG GEIVIYPPKN
IHINTTDSAI IGNTCLYGAT GGALYAAGTA GERFAVRNSG SHAVVEGAGD HCCEYMTGGV
VTVLGKTGLN FGAGMTGGFA YVLDMQGDFF DRCNHELIDL HRISSEQTEE HRIYLRKIIE
THVEKTDSAW GKTILSDFEH YVRKFYLVKP KAANIATLLK STLADPQ
//
