ID A4X9M7_SALTO Unreviewed; 1573 AA.
AC A4X9M7;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ABP55601.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:ABP55601.1};
GN OrderedLocusNames=Strop_3167 {ECO:0000313|EMBL:ABP55601.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55601.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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}.
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DR EMBL; CP000667; ABP55601.1; -; Genomic_DNA.
DR RefSeq; WP_012014378.1; NC_009380.1.
DR STRING; 369723.Strop_3167; -.
DR MEROPS; C44.003; -.
DR KEGG; stp:Strop_3167; -.
DR PATRIC; fig|369723.5.peg.3258; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABP55601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000235}.
FT DOMAIN 35..440
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1573 AA; 169828 MW; 17B794A39686B4D7 CRC64;
MAVPYPHRIP QQVPHPGPNG STAGLYDPAY ERDACGVAFV ADLRGRRSHG VVANGLAALR
RLDHRGARGA EPNTGDGAGI LIQVPDALLR AVVDFPLPPI GEYATGLVFL PDDDEAELRA
RRVVEKYALV EGADLLGWRD VPVDPAGLGA TAHAAMPRVR QIFVTAHRLT DSTTGPAGSR
LTGLELERVA YCVRRQAERE SAERGVPAYF PSLSGRTMVW KGMLTPDQLP EFYPELTDER
MCSAIALVHS RFSTNTFPSW PLAHPFRFIA HNGEINTIRG NRNWMQARES MLAGGAGAAL
PGNIRRIFPV CTPGVSDSAN FDEVLELLHL AGRSLPHAVL MMIPEAWEND PDMPADQRAF
YRFHASLMEP WDGPASVAFT DGEIVGAVLD RNGLRPGRWW QTSDGLVVLG SEAGVLDLDP
ATVVAKGRLQ PGRMFLVDTV GGRIVHDDEI KAELAAAQPY EEWLHAGLIE LTDLPAREHI
VYTHDSVRRR QQAFGYTEEE LKILLAPMAR VGAEPIGSMG TDTPISPLST RPRLLYDYFH
QLFAQVTNPP LDAIREELVT SLQSTVGPEG NLLDPGPASC RQLELPYPVI DNDELAKILS
IDEDGNLPGF KAVRVSGLYR IREGGAGIRA RLTEICRHVS EAIEDGVRIL VLSDRDSNAN
LAPIPSLLLT AAVHQHLVRE QTRTQVSLIV ESGDCREVHH AAVLVGYGAV AVNPYLAFES
VEDMISTGAL VGVEPGTAVR NYVRALGKGV LKIMSKMGIS TVSSYCGAQV FEAVGLDSQL
IERYFRGTPS KIGGIDLDGI HVEVAARHAL AWPAPGAATS DRLDVGGEYQ WRREGELHLF
NPETVFLLQH ATRSRQYDVF RAYTSKVDAL AAQGGALRGR FALRTGVRPP VPIEEVEPAS
EIVRRFATGA MSYGSISVEA HETLAVAMNR LGGKSNTGEG GEDVQRLYDP TRRSAVKQIA
SGRFGVTTEY LVNADDLQIK MAQGAKPGEG GQLPGNKVWP WIARTRHATP GVGLISPPPH
HDIYSIEDLA QLVHDLKCVN PAARVHVKLV SEVGVGTVAA GVAKLKADVI LISGHDGGTG
ASPLNSLKHA GTPWELGLAE AQQTLLLNKL RDRVTVQVDG QLKTGRDVLV AALLGAEEFG
FATAPLIVEG CVMMRVCHLD TCPVGIATQN PVLRERFTGR PEFVENFFLF LAEEVRGYLA
ELGLRSIDEA IGRTELLDVA PAVDHWKAVG IDLSPVLRLP ELPEETARRG VRAQDHGLGL
ALDNELIALA EPALRAGSRV RTQLSVRNEH RSVGAMLGGE VVRRHGGAGL PTDTIEFDLH
GTVGQSFGAF LPSGVTLRLH GDANDYVGKG LSGGRLVLRP DRASPFVNVE TMPGRRAEDQ
IIAGNTILYG ATAGEVFLRG RVGERFAVRN SGAAAVVEGV GDHGCEYMTG GTIVVLGPTG
RNFAAGMSGG TAFVWRLDRR RVNTELVDLT PLSEQEQATL YDLVQRHFTE TDSAVAEDLL
KRWSEAVEEF TAVVPRDYRR VLEIMRAAEA AGYDVDDAVM SALAAPATQP TSSGPSTPVS
PVSQMAAQEV ARA
//
