ID A0A161LAE2_9ACTN Unreviewed; 1505 AA.
AC A0A161LAE2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:GAT64754.1};
GN ORFNames=PS9374_00386 {ECO:0000313|EMBL:GAT64754.1};
OS Planomonospora sphaerica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Planomonospora.
OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT64754.1, ECO:0000313|Proteomes:UP000077701};
RN [1] {ECO:0000313|EMBL:GAT64754.1, ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT64754.1,
RC ECO:0000313|Proteomes:UP000077701};
RA Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT Actinomycete.";
RL Genome Announc. 4:e00779-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA Suzuki T., Dohra H., Kodani S.;
RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL Submitted (APR-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:GAT64754.1}.
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DR EMBL; BDCX01000001; GAT64754.1; -; Genomic_DNA.
DR STRING; 161355.PS9374_00386; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000077701; 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:UP000077701}.
FT DOMAIN 24..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1505 AA; 162609 MW; A61C1A2BA284831F CRC64;
MPAAHLGFPE PQGLYDPAHE HDACGVAMVA DVAGRRSHDI VAKALTALCN LDHRGAQGSE
PDTGDGAGIL TQIPDTFLRA VAAEAGLREL PPAGSYAAGT AFLPIDAEAR ATAERMIEEI
AAEEGLTVLG WRDVPVDPTL PGPSARAVMP FFRQLFVSSP GGESGLELDR LAFCLRKRAE
HEADVYFPSL SSRTIVYKGM LTPGQVEPFF PDLSDERYET AISLVHSRFS TNTFPSWPLA
HPYRYVAHNG EINTVKGNRN WMRAREAMLE TANLPGDLAR LFPICDPDSS DTGSFDEALE
LLHLAGRTLP HAVLMMIPEA WENHTEMDPA RRAFYEFHSS LMEAWDGPAS ITFSDGTLVG
AVLDRNGLRP GRFWVTDDGL VVLASEAGVL DIEPERVVRK GRLQPGRMFL IDTARGKIIE
DDEIKAELAA ELPYAEWLHA GLVRFEELPA RSREIPTHEA LVKRQQTFGY TEEELRIILS
PMARTGAEPI GSMGTDTPVA VLSEKPRLLF DYFSQLFAQV TNPPLDAIRE ELVTSLASTI
GPEGNLLDPG PASCRQLVLP YPVIDNDELA KIIHINDEGA LPGFQPYVVS GLYEVAGGGQ
ALVRRLTEIR AEVSAAIAGG ARIIVLSDRG SSAELAPIPS LMLTGAVHHH LIAEKTRTRV
GLVIETGEAR ECHHMALLIG YGAGAVNPYL AIETVEDMVD TGVLKVDRHK AVRNLIKAYG
KGVLKVMSKM GVSTVASYTG AQIFEALGLG QEVVDTCFAG TTSRLGGVGF DVLARETAER
HLRAYPRVEN AHRRLEVGGE YQWRREGEPH LFNPETVFKL QHATRTRRYE IFKEYTGLVD
SQAERLMTLR GLFRFRDGVR EPVPIDEVEP VSEIVKRFST GAMSYGSISA EAHETLAIAM
NRLGGKSNTG EGGEDPERLY DPARRSSIKQ VASGRFGVTS EYLVNADDIQ IKMAQGAKPG
EGGQLPGHKV YPWIAKTRHS TPGVGLISPP PHHDIYSIED LAQLIHDLKN ANPVARVHVK
LVAEVGVGTV AAGVSKAHAD VVLISGHDGG TGASPLTSLK HAGAPWELGL AETQQTLLLN
GLRDRITVQV DGQLKTGRDV VIAALLGAEE YGFATAPLVV SGCVMMRVCH LDTCPVGVAT
QNPELRRRFT GRPEFVVNFF EFIAEEIREY LAQLGFRSLE EAIGHAELLD TASAEDHWKA
AGLDLGPILH QPELPEGAAV RKVREQDHGL DAALDNTLIQ LAEGALADGT PVTLDLPIRN
VNRTVGTMLG HEVTKRYGGA GLPDGTIDVR FTGSAGNSFG AFVPRGITLR LTGDANDYLG
KGLSGGRIIV RPHEAAPLDG HIIAGNVGLY GATSGEAFVR GVMGERFCVR NSGATAVVEG
VGDHGCEYMT GGRVVVLGPT GRNFAAGMSG GIAYLLDLDP ARVNREMVEI EPLGEADSEE
LRKIVEAHLA ETGSPVAREL LADWDPARFS KIMPTDYKRV LRAAEAARLE GRDIDEAVMT
AAVQG
//
