ID A0A0A5I1K0_9BACI Unreviewed; 1520 AA.
AC A0A0A5I1K0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KGX89737.1};
GN ORFNames=N781_16080 {ECO:0000313|EMBL:KGX89737.1};
OS Pontibacillus halophilus JSM 076056 = DSM 19796.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX89737.1, ECO:0000313|Proteomes:UP000030528};
RN [1] {ECO:0000313|EMBL:KGX89737.1, ECO:0000313|Proteomes:UP000030528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX89737.1,
RC ECO:0000313|Proteomes:UP000030528};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX89737.1}.
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DR EMBL; AVPE01000020; KGX89737.1; -; Genomic_DNA.
DR RefSeq; WP_036770562.1; NZ_AVPE01000020.1.
DR STRING; 1385510.GCA_000425205_02214; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000030528; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030528}.
FT DOMAIN 23..416
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1520 AA; 168338 MW; 10D14E637A0B17B9 CRC64;
MTSYNKMPDA QGLYHPEFEH DACGIGLYAS LKGEATHEIV QKGLHMLCQL DHRGGQGSDP
YTGDGAGIMI QIPHTYFSKV MSPIQLPEQG RYGVGMIFFG NDEHRAESEA KIEAYIEQEG
QSLLGWRDVP INVGKLGQSA KDTVPVIRQV FIGASDELQD DLAFERKLYV IRKQAANWSN
QHGREFYFAS LSSRTIVYKG LLLPEQVDQF YLDTQDEDFV SPFSLVHSRF STNTFPSWER
AHPNRYLIHN GEINTMRGNT NWMKAREHQI ASDAFGDDLE KLLPILNESG SDSSILDNAF
EFFVLAGRSP AHTAMMLIPE PWAQNPHMSP ERRAFYEYHS SMMEAWDGPT SITFTDGKQI
GAILDRNGLR PARYYVTKDD MIIYSSEVGV IDDLEEDNIL YKNRLSPGKM LLIDLEEHRI
ISDEEIKSQM ASAEPYQQWL DENLLKLERG SRLVEEESAE EIFLRQRAFG YTYEDLDKYL
LPLVTEGKDP IGAMGNDAPL AVLSDRPQSL FNYFKQLFAQ VTNPPIDSLR EKLVTSTMTL
LGAEGDILHP DASNCRRIQV DSPVLSYSQV DHIRNNDVAE FKSHTINVLF RQDLKEELKL
ICEEAEQALK DGASLLILSD KGMNKDLVPV PPLLAVSALH QHLVKKGVRT KASILVESGE
VREVHHFAAL IGYGADAIYP YLAYESFRYM IDQEHLDLEL DVAVDRYMSS VTTGIVKVMS
KMGISTVQSY RGAQIFEAVG IGQSVMDEYF TGTASQLGGV GLDVLSEEAI RRHDTAYQDV
LSTALDSGSD FQWRHNGEFH AFNPKTIHTL QWACRREDYS LFKEYSTAAN EERMSFLRNL
FQFKKRDAVP LEEVESVDSI VKRFKTGAMS FGSLSQEAHE ALAIAMNRLG GKSNSGEGGE
DPDRYTVDEN GDLRRSAIKQ VASGRFGVNS HYLVNADEIQ IKVAQGAKPG EGGQLPGKKV
YPWVGAVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN ANRAARINVK LVAKSGVGTI
AAGVAKGAAD VITISGYDGG TGASPKTSIK HTGLPWELGL AEAHQTLMLN NLRERVTLET
DGKLMTGKDV VMAALLGAEE FGFGTAPLVV LGCIMMRVCH KDTCPVGVAT QNPELRAKFM
GSPDHIVNYM RFVAQEVREY MSELGFRSMD EMVGRTDVLG VSERASSHWK AKHLDLTRLL
HRVEGGRVFR TEQDHKIHAS LDLNTLLPKV QRSIETGERI EVESKIRNVN RVVGTIVGSE
VTKRYGAKGL PDDTIRLRFT GSAGQSLGAF LPKGISILLT GDANDYVGKG LSGGKIAVAA
PRQVNASSND IIIGNVAFYG ATAGEAYING YAGERFAVRN SGADVVVEGV GDHGCEYMTG
GRVVVLGEVG KNFGAGMSGG TAYVFAEDKA QFQSLCNDGM IEFESLQDKE EMEELKRLVR
NHYLHTGSLK ASRLLSTWET SVAQFVKVIP KDFKEMLGHI EEQRQLGYSE KDAVLRAFLN
KTGQKMNDAA PDQMKEPLVN
//
