ID A0A0P4RHQ2_9ACTN Unreviewed; 1540 AA.
AC A0A0P4RHQ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative glutamate synthase large subunit {ECO:0000313|EMBL:GAO12799.1};
GN Name=gltB {ECO:0000313|EMBL:GAO12799.1};
GN ORFNames=TPA0598_12_01670 {ECO:0000313|EMBL:GAO12799.1};
OS Streptomyces lydicamycinicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO12799.1, ECO:0000313|Proteomes:UP000048965};
RN [1] {ECO:0000313|Proteomes:UP000048965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAO12799.1, ECO:0000313|Proteomes:UP000048965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO12799.1,
RC ECO:0000313|Proteomes:UP000048965};
RX PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT producer of anti-MRSA antibiotic lydicamycins.";
RL Stand. Genomic Sci. 10:58-58(2015).
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:GAO12799.1}.
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DR EMBL; BBNO01000012; GAO12799.1; -; Genomic_DNA.
DR RefSeq; WP_042162155.1; NZ_CP098437.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000048965; 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:UP000048965}.
FT DOMAIN 41..433
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 165534 MW; 70FB11C13A4A46F3 CRC64;
MRFASTHSAT TSSSDAAAWS PMDGRPAQQG MYDPRNEHDA CGVGFVATLT GEASHALVEQ
ALTVLTNLEH RGATGSEPDS GDGAGILLQV PDAFLRENVT FELPEAGAYA VGIAFLPSDA
QEAAEAVSRI ETIAGEEGLD VIGWRVVPVA PQLLGNGARA TMPAFSQIFV SDGVNTGLAL
DRKAFALRKR AEREAGVYFP SLSARTIVYK GMLTTGQLEP FFPDLSDRRF ATAIALVHSR
FSTNTFPSWP LAHPYRFVAH NGEINTVKGN RNWMRARESQ LATKLFGAEN GEDAENLSRL
FPVCTPDASD SASFDEVLEL LHLGGRSLPH SVLMMVPEAW ENSPSMDPAR RAFYQYHSTM
MEPWDGPACV TFTDGIQVGA VLDRNGLRPG RYWVTDDGLV VLSSEVGVLD IDPAKVVRKG
RLQPGRMFLV DTVEGRIIED DEIKAQLAAE QPYQEWLDSG LIELADLPER EHIVHTHASV
TRRQQTFGYT EEELRVILAP MAKAGAEPIG SMGTDSPIAA LSERPRLLFD YFTQLFAQVT
NPPLDAIREE LVTSLISSLG PQGNLLEPTA ASCRSVTLPF PVIDNDELAK LVHINADGDM
PGMKAVTLSG LYRVSGGGES LAARIEEICA EADAAIDDGA RLIVLSDRHS DAEHAPIPSL
LLTAAVHHHL IGTKERTQVG LLVEAGDVRE VHHVALLIGF GAAAVNPYLA MESVEDLVRA
GTFLPGVEAE TAIKNLIKAL GKGVLKVMSK MGISTVASYR GAQVFEAVGL DEEFVEKYFH
GTATKIGGAG LDVIAKEVAA RHAKAYPASG IAATHRALEI GGEYQWRREG EPHLFDPDTV
FRLQHSTRSR RYDIFKQYTD RVNEQSERLM TLRGLFSFAS DRPSIPIEEV EPASEIVKRF
STGAMSYGSI SQEAHETLAI AMNQLGGKSN TGEGGEDPER LYDPARRSSI KQVASGRFGV
TSEYLVNSDD IQIKMAQGAK PGEGGQLPGH KVYPWVAKTR HSTPGVGLIS PPPHHDIYSI
EDLAQLIHDL KNANPQARIH VKLVSEVGVG TVAAGVSKAH ADVVLISGHD GGTGASPLTS
LKHAGGPWEL GLAETQQTLL LNGLRDRIVV QTDGQLKTGR DVVIAALLGA EEFGFATAPL
VVSGCVMMRV CHLDTCPVGI ATQNPTLRER FSGKAEYVVN FFQFIAEEVR ELLAELGFRS
LDEAIGHAEL LNTSRAVDHW KAQGLDLAPL LHVPELAEGA VRHQVIEQDH GLEKALDNEL
IKLAADALSA DSAEAAQPVR AQVAIRNINR TVGTMLGHEV TKKFGGAGLP DDTVDITFTG
SAGQSFGAFL PRGITLRLEG DANDYVGKGL SGGRVIVRPD RGADHLAEYS TIAGNTLAYG
ATGGELYLRG RVGERFCVRN SGATVVSEGV GDHGCEYMTG GNAVVLGETG RNFAAGMSGG
FAYVIDLDKA NVNKELVDAV HALDDADKQW LHDVVRRHQE ETGSTVAEKL LADWDAAAAR
FSKVIPPIYK AVLAAKDAAE QAGLSESETH EKMMEAATNG
//
