ID A0A0Q3WQ25_BRECH Unreviewed; 1537 AA.
AC A0A0Q3WQ25;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQL49567.1};
GN ORFNames=AN963_07475 {ECO:0000313|EMBL:KQL49567.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL49567.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL49567.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL49567.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL49567.1}.
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DR EMBL; LJJB01000007; KQL49567.1; -; Genomic_DNA.
DR RefSeq; WP_055743875.1; NZ_LJJB01000007.1.
DR STRING; 54911.AN963_07475; -.
DR PATRIC; fig|54911.3.peg.5646; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000051063; 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 22..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1537 AA; 168555 MW; 41D926EFA1D54C2C CRC64;
MSMRGLPTKQ GLYDPMFEHD ACGIGFIANL KNKANHEMVS KGLQILCHLE HRGGQGSDPE
TGDGAGILTG IPHTFFKKSC DELGFKLPAQ GKYGVGMLFL PMDETLRNTY EKQLEEIIQA
EGQKLLGWRT VPTNTDKIGK TAKASQPFVR QVFIGASSTV KDQLSFERKL YIIRKQMEQV
AREGFYAASM SSRTIVYKGL VTPEQLDQFY TDLQDESYAS PFSVVHSRFS TNTFPTWERA
HPNRYLIHNG EINTLQGNIN WMRAREQMFQ SEAFGSDLQK VVPVIDLEGS DSAILDNCVE
FFSLAGRSLP HVAMMMIPEP WDQDANIEAS KKAFYEYHSC LMEPWDGPTA ISFTDGKQIG
AILDRNGLRP ARYYVTSDDT IIFSSEVGVL EVPDEKIVQK GRLSPGKMLL VDLEEGRIVS
DEEIKQQIAN EQLYGEWVQK NLVTLTALPK ANTPARIAGD TLLARQKAFG YTQEELTKVL
TPMVAEKKDP IGSMGIDTPL AVLSDRPQLL YNYFKQSFAQ VTNPPIDALR EACVTSTLSY
LGAEGNLLAP DESNCRRIRL SSPLLSNEEL AKLASNPHLE FQAKALPILF PADGGATGLE
IALDDLFAAA DQAMESGHTL LILSDRGMNE KQAAIPALLA GSGLHHYLVS KGTRTQVSVI
VESGEPRDVH QFAMLIGYGV DAVNPYVAID SLLELAASEK GNGVNAKDAV EIYMRTAVEG
VVKVMSKMGI STVQSYRGAQ IFEAIGIDSS VIDRYFTRTA SKIGGITLEV IAKETLARHA
KAFLPEHSEE NLDPGSDFQF RRDGEFHLFN PKTVHALQKA VREGSYEQYK LYSEMANDQQ
FAFLRHLLDF KSDRMPVPLN EVESVDSIVH RFKTGAMSYG SLSKEAHETL AIAMNRLGAK
SNSGEGGEDP QRYMIDENGD LRRSAIKQVA SGRFGVSSHY LVNASEIQIK MAQGAKPGEG
GQLPGNKVYP WIAEVRKSTP GVGLISPPPH HDIYSIEDLA QLIFDLKNAN PRARISVKLV
SKAGVGTIAA GVAKGLADVI VISGHDGGTG ASPKSSIKHA GLPWELGLAE THQTLLLNQL
RDRVVVETDG KMMTGRDVVI AALLGAEEFG FATAPLVSIG CVMARVCHLD TCPVGVATQN
PDLRKKFKGD PQHAVNFVRF VAREVREIMA ELGFRSFEDM IGRSQLLTMN EKAKSHWKAK
HIDLSLLLFQ PEVPEEVGRF HQRSQDHKLD ATLDRQQLLA LSKPALEKQR QVEINLPINN
TNRVVGTILG SEVTRRFGEH GLPEDTIRLN FKGSAGQSFG AFVPRGITLK LEGDANDYVG
KGLSGGRLAV YPSKKVTYAP EKNMIIGNVA FYGATSGEAY ISGMAGERFC VRNSGMTAVV
EGVGDHGCEY MTGGRVVVLG QVGKNFAAGM SGGTAYVLAE DKAVFTALCN QEMVLLEALQ
DEREAAEVKK LLENHVANTG SQHAHALLNQ WEQTKAKFVK VIPKDYKQII LTMEELQQSG
MKRSDAILAA FEISQKKNVE KAPKAKTEEQ VAASVGK
//
