ID A0A1S2QWC5_9BACI Unreviewed; 1489 AA.
AC A0A1S2QWC5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:OIK09826.1};
GN ORFNames=BIV60_22755 {ECO:0000313|EMBL:OIK09826.1};
OS Bacillus sp. MUM 116.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK09826.1, ECO:0000313|Proteomes:UP000180019};
RN [1] {ECO:0000313|EMBL:OIK09826.1, ECO:0000313|Proteomes:UP000180019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 116 {ECO:0000313|EMBL:OIK09826.1,
RC ECO:0000313|Proteomes:UP000180019};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 116.";
RL Submitted (OCT-2016) 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:OIK09826.1}.
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DR EMBL; MLYR01000104; OIK09826.1; -; Genomic_DNA.
DR RefSeq; WP_071358007.1; NZ_MLYR01000104.1.
DR STRING; 1678002.BIV60_22755; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000180019; 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; cd02808; GltS_FMN; 1.
DR CDD; cd00504; GXGXG; 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:UP000180019}.
FT DOMAIN 21..391
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1489 AA; 163479 MW; 0808FFDFAF245D83 CRC64;
MTLKYNPSKF KDFHKHEHDS CGIVACLEKH KIPTRKNIFD CIDALVTMNH RAGFINGEGD
GVGIHMDIPV ALWKEKLQNA GIDPQLAEKE EFAVGHVFIS QKVNWHSTKN ELLQKLEKYE
LELVFETVDV TDSSALGPIA IQENPVFWQF ACLSKKSGQE LTKVLFEALV DFELNDHIHV
ASFSQSHVVY KVMGAGDILP RYYKDLANPL AASTITLGHN RYSTNTLSSF FRVQPFSVLG
HNGEINTIAK LRDEARMIGV PLVKDGSDSQ DLSRTMETLI SRDGYSLFEV MDLLFPPIIN
EIKAYPDKLQ DLYTYLREAW GHYAQGPAGI ISRYGDEAVF SVDALGLRPL WMLETETSYL
FSSEPGIIPS SEYVNDPKPL APGEKVGFKW NGDQLDVYEQ NRFQNEVYNR ISNQLNIENS
RNRLKSPSLN KTVTMNYPDK IHNGQYKAFG WERDHIQLIE QMAEKGIEPI RSLGHDAPLA
ALNPERKNIA DFFKESVAVV TNPAIDRDRE TEHFSTRVIL GKRPSLFEKE ETNTVLELIT
PILLEGKSGF VCSEELVQPS FDQVVQYYNE QKLATFISAT FRKDEDINLA LERLASEAVQ
AVQSGKILLV LDDAKAHQED FYWIDPHLVT SAIDQALVKA ELRRDCSLVL RSASIRSLHD
IITALGLGAD LISPYYMFMT VLDESTKPLT NLYSALTKGL EKVISTIGIH ELRGYGRLFS
SIGLHDDIAK VLNIVNFFGS MEIELDFETM KQDSIARAQD YHNEKERIGK TFHLFPRIWK
AIGDVAATGD YSVYRDKISE QELGNPTTIR HLAGLKVSNH PISPTEVDIT VGEHDLPFVI
SSMSFGSQNE IAFRAYAEGA DRLNMVSLNG EGGEIKDMLG KYPKTRGQQI ASGRFGVNAE
LLNSSNLLEI KIGQGAKPGE GGHLPGSKVT AKVAAARNAT LGSDLISPSN NHDIYSIEDL
AQMILELKTA NDQAKISVKV PVVPNIGTIA VGIAKAGADI ITLSGFDGGT GAARIHALQH
VGLPVEIGVK AAHNALLESG LRHKVEIWAD GGMKSAMDVM KIMLLGANRI GFGTLAMLSI
GCTTCRGCHL DTCHVGIATQ IESEIQAKEH GLRRFVPRQF DLAVQGIMNL FTAFGQELKT
LAASLGIRNL QEAVGRSDLL FQTSGNQKLD LSYLLKPLEI TQFTKAEASK TIAETQMQVA
VGAEYLDASI DQLHSSREFV SVTSEQRVLG SRVSCHRVRG RVDGSYKQLQ PVQLKYREGS
IPGNGLGAYN SEGIFITVNG GGQDGVGKTS FGGNIQILKA KGKNGRYYNG SVGKGFGYGA
QKGLLVAQGN ADARAGIRLS GADLIIGGAV KQPIPAQENG NIGAGANIKG FAFEYMTNGR
GLVLGDPGPW ICAGMTGGVV YTRHQPEMGL TKEAIQRRIA KGAKVSVNPL DKKGKTDVQE
LLGQYISLLE NDGQVEEATQ LQALLPTLEE HFVQIVPVKE QADPSVSTE
//
