ID K6W027_9ACTN Unreviewed; 1527 AA.
AC K6W027;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:GAC01854.1};
GN Name=gltB {ECO:0000313|EMBL:GAC01854.1};
GN ORFNames=GONAM_35_00240 {ECO:0000313|EMBL:GAC01854.1};
OS Gordonia namibiensis NBRC 108229.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1208314 {ECO:0000313|EMBL:GAC01854.1, ECO:0000313|Proteomes:UP000035058};
RN [1] {ECO:0000313|EMBL:GAC01854.1, ECO:0000313|Proteomes:UP000035058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108229 {ECO:0000313|EMBL:GAC01854.1,
RC ECO:0000313|Proteomes:UP000035058};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia namibiensis NBRC 108229.";
RL Submitted (AUG-2012) 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:GAC01854.1}.
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DR EMBL; BAHE01000035; GAC01854.1; -; Genomic_DNA.
DR RefSeq; WP_006868014.1; NZ_BAHE01000035.1.
DR Proteomes; UP000035058; 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..417
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 910..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1527 AA; 165717 MW; DD8143C4B22D711A CRC64;
MKQAPGPVGL YDPRNEHDSC GVAFVVDMHG RRSRDIVDKA IMALVNLEHR GAAGAEPNTG
DGAGIMIQVP DRFLRETVDF ELPAEGSYAT GIAFLPQGSE DARLACEGVE KVIESEGLTL
LGWREVPTNE NSLGALARDA MPTFRQVFIG GAEGMELERR AYVVRKRVQY ELGNKGAGAD
GPGRETVYFP SLSGRTFVYK GMLTTPQLRE FYVDLQDSRV ESSLGLVHSR FSTNTFPSWP
LAHPFRRVAH NGEINTVTGN ENWMRAREAL INTEAFGADA ASKIFPICTP GASDTARFDE
VLELLHLGGR SLPHAVLMMI PEAWERHESM KPEHRAFYRY HSALMEPWDG PASVCFTDGT
VVGAVLDRNG LRPSRIWVTK DGLVVMASEV GVLDIDHADV VQKMRLQPGR MFLVDTAAGR
IVDDEEIKDE LAAEHPYAEW LEKGMVAVDD IEAQPHVHMP HDRVALRQQV FGYTSEELNL
LVAPMAKTGA EALGSMGTDT PIAVLSKRPR MLFDYFQQMF AQVTNPPLDA IREEVVTSVG
STIGSEADLL NPSPVSCRQI ELPQPVIDND TLAKLVQIND NESLPDFRSV HIHGLYPVAE
GGAGLRKALD EIRAKASAAI EDGANLIVLS DRESDENLAP IPSLLLTAAV HHHLVRERKR
TRAGLIVESG DCREVHHVAT LVGFGAAAVN PYMAFESIED MVERGVLGDV DFATAKKNYI
KAASKGVLKV MSKMGISTIA SYTGAQLFQV IGLSQATVDE FFTGLISQLD GIGLDEIAAD
VAARHALAFS DRPSERAHRE LEVGGEYQWR REGEYHLFNP DTVFKLQHST RTGQYGVFKE
YTKMVDDQST RLGTLRGLFD FNFGDRDPIP IEKVEPASEI VKRFSTGAMS FGSISAEAHE
TLAIAMNRLG GRSNSGEGGE DPRRFHHDEN GDWRRSAIKQ VASGRFGVTS HYLSNCTDIQ
IKMAQGAKPG EGGQLPPHKV YPWVAEVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN
ANPKARIHVK LVSEVGVGTV AAGVSKAHAD VVLISGHDGG TGASPLTSLK HAGAPWEIGL
AETQQTLLLN GLRDRIVVQV DGQMKTGRDV VIAALLGGEE FGFATAPLVV SGCVMMRVCH
LDTCPVGIAT QNPLLRERFA GKPEFVENFF LFIAEEVREL LARLGFRTLQ EAVGHVEALD
TTKALAHWKS EKAGKLDLTS ILTMPESPFM NQDLYCSGVQ DHSLEKALDQ QLIAQSRDAI
DHGTRVSFTS KITNVNRTVG TMLGHEVTKT YGAQGLPDGT IIVDFTGSAG NSFGAFVPKG
ITLRLEGDAN DFVGKGLSGG RLVVRPARNA PADFVAEDNI IAGNVIGFGA TAGKIFLRGI
VGERFCVRNS GATAVVEGVG DHGCEYMTGG RVVVLGETGR NFAAGMSGGM AFVYDPDAKL
ADNLNTELVD LEPLEAEDIE FLAAIIDEHR AETESPVAAA LLADWDTAQT KFAKVMPRDY
KRVLLAISEA EKTGRDVNEA IMEAARG
//
