ID A0A256B931_9CYAN Unreviewed; 1529 AA.
AC A0A256B931;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OYQ62349.1};
GN ORFNames=B9G53_22710 {ECO:0000313|EMBL:OYQ62349.1};
OS Pseudanabaena sp. SR411.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=1980935 {ECO:0000313|EMBL:OYQ62349.1, ECO:0000313|Proteomes:UP000215660};
RN [1] {ECO:0000313|EMBL:OYQ62349.1, ECO:0000313|Proteomes:UP000215660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR411 {ECO:0000313|EMBL:OYQ62349.1,
RC ECO:0000313|Proteomes:UP000215660};
RA Stowe E.L., Hundermark E.L., Stowe W.;
RT "Novel uncharacterized cyanobacterium from Susquehanna River.";
RL Submitted (APR-2017) 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:OYQ62349.1}.
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DR EMBL; NDHW01000212; OYQ62349.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000215660; 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:UP000215660}.
FT DOMAIN 22..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1529 AA; 166695 MW; 44AD3CD746B7E1A0 CRC64;
MNSNALPLKQ GLYDPQFEHD ACGVGFIVHK SGKKSHAIVE QGLTILENLE HRGACGCETN
TGDGAGILMQ IPHKFLVKVA AAANITLPEA GQYGVGMVYA SPDSNTRKNG REAFEKLVAA
EGLKVLGWRD VPTDNSSLGA TAQSSEPFMQ QVFIGRSPDL ADDLAFDRKL FVLRKLAHTA
IRAANVDPYW YPSSLSCRTI VYKGMLMTAQ VGMYYAHDLR DPDMESALAL VHSRFSTNTF
PSWERSHPYR YIAHNGEINT LRGNTNWMIA RQSMFESDLF GDDISKIKPV INIEGSDSTI
FDNALELLVL AGRSLPHAVM MMIPEPWTAH ESMSDEKKAF YEYHSCLMEP WDGPASIAFT
DGTMIGAVLD RNGLRPSRYY VTKDDLVIFA SEAGVLDIAP EMIESKGRLQ PGRMFLVNME
EGRIVADEEI KHQIATEHPY RDWINQHMVD IANLKDGVAS EPEAIPLTQK QMAFGYSFED
LRLLLTPMAR DGVEAIGAMG ADTPLAVLSN RPKLLYDYFQ QLFAQVTNPP IDSIREEIIT
SAETTIGAER NLLKPEPESC HLIELKTPIL SDAEFAKLKH INEGGFKSIT LSTLFNPKSG
VAGLESVITE ICTKADQAIA DGVNILILSD RGVNPDNAPI PALLAVSGLH HHLIRTGTRT
RVGLVLESGE PREVHHFALL IGYGCGAINP YLAFETIKDM IDQRLLVNVE FKTAVKNFIK
SATKGVTKVA SKIGISTIQS YRGAQIFEAV GLNQDVIKKY FTWTASRIEG ADLEVIAKEA
IARHTHAFPD RPASGNTLDV GGDYQWRKDG EAHLFSPETI HALQKAVRDG NYELFKKYSA
LVNEQNQQHF TLRGLLDFKA RESISIDEVE PIESILSRFK TGAMSYGSIS KEAHEALAIA
MNRIGGKSNT GEGGEDPDRY TWTNEQGDSK NSAIKQVASG RFGVTSLYLS QAKEIQIKMA
QGAKPGEGGQ LPGKKVYPWI AKVRHSTPGV GLISPPPHHD IYSIEDLAEL IHDLKNANRA
ARISVKLVSE VGVGTIAAGV SKAHADVVLI SGYDGGTGAS PQTSIKHAGL PWELGLAETH
QTLVLNNLRS RIVVETDGQM KTGRDVVIAA LLGAEEFGFA TAPLVTLGCI MMRVCHLNTC
PVGVATQDPQ LRDKFTGDPA HTVNFMTFIA MEVRELMAKL GFRTLDEMVG RTEVLEAKQA
VEHWKAKGLD FSKILYQPEV GAEVGRYCQI PQDHGLDKSL DMTVLLDLCQ AAIVDGEPVQ
ETIPIKNINR AVGTILGNEI TKRHWEGLPD DTVHLHFQGT AGQSFGAFVP SGVTMELEGD
TNDYLGKGLS GGKIILYPDK ASTFVAEENV IAGNVALYGA TSGEVYIRGI AGERFGVRNS
GVNAVVEGIG DHGCEYMTGG KVVVLGLTGR NFAAGMSGGV AYILDESGDF ATRCNTSMVG
LEKLEDPEEI KDLKQLIQQH VDYTESAKGA KVLADWNAIV PKFVKVMPKD YKRVLQAIKE
ALEDGLSGDD ALNAAFEANS RDVARIGGS
//
