ID A0A0S2K986_9GAMM Unreviewed; 1524 AA.
AC A0A0S2K986;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:ALO44858.1};
GN ORFNames=PS2015_163 {ECO:0000313|EMBL:ALO44858.1};
OS Pseudohongiella spirulinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudohongiellaceae; Pseudohongiella.
OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO44858.1, ECO:0000313|Proteomes:UP000065641};
RN [1] {ECO:0000313|EMBL:ALO44858.1, ECO:0000313|Proteomes:UP000065641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO44858.1,
RC ECO:0000313|Proteomes:UP000065641};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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}.
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DR EMBL; CP013189; ALO44858.1; -; Genomic_DNA.
DR RefSeq; WP_058020382.1; NZ_CP013189.1.
DR STRING; 1249552.PS2015_163; -.
DR KEGG; pspi:PS2015_163; -.
DR PATRIC; fig|1249552.3.peg.167; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000065641; Chromosome.
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:UP000065641}.
FT DOMAIN 29..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1524 AA; 167207 MW; 22ECD1A5A6C5D33E CRC64;
MTDQAQFPSQ IGFPDKTGLY DPANEKDACG VGFVADIKGR PSHQIMLDAY HLNSRMDHRG
GCGFEANTGD GAGILMALPH SFFADIAKKE LDTTLPAHGH YATGNIFLPQ NTKEREYCRD
AINQIIAEEG QVLIGWRDVP VDAEGADVGP AARAAQPKIE QLFIGAADGL DQEAFERKLY
IIRKRFTHKL RGDSSLTQAK MVYACSLSTK VIVYKGMLTP GQLFPFYQDL TNPACETHMA
MVHSRFSTNT FPSWDRAQPN RFMSHNGEIN TLRGNVNWMV AREGTLETDL FGDKLKDLFP
IIDSDCSDSG SFDSVLEFML LSGRSLQEAV MMMIPEAWQS DVNMSQDKKD FYEFHSALME
PWDGPASIVF SDGHYIGAVL DRNGLRPSRY YVTHDDKVIM ASEVGVVQVD PANVKLKGRL
QPGRMFLLDF EQGRLIPDEE LKHSIAAKRP YGEWLQNQRI TLEMLADGNE AHSLDSEDVL
QRMQAFGYTT ETMQFMLLPM ITEARDPLGS MGNDSALACL SDKPRMIYDY FKQLFAQVTN
PAIDSIREEV VMSLECFIGP EGNLLETTEQ HAHRLSLKHP ILSNKQLQTI RGMDHNGLRS
KVIDITYDAH AENGYLNALE RICKEASRAI AEGFAFVILS DRKIDKNRIA ISALVATGAV
HHHLIRTHER TKIGLIVETG EAREVHHHCL LVGYGADAIN PYLAFEAIWQ AQLDGLLGKD
YPNESDVVYA YKKAVAKGML KVMAKMGIST LQSYRGAQIF EAVGLAEEVV NRCFVGTASR
VQGVNFATLV EETERRHRIG FPANDENRIP VLNNPGDFHW RNNGDSHMWD PTAIFNLQNA
ARTNSPDAYK AFAKYTNEQT TRACTLRGLL KFRDNQQAIP LDEVEPAKEI VKRFATGAMS
FGSISQESHE ALAVAMNRLG GKSNTGEGGE DPIRFQPLPN GDSKRSAIKQ VASGRFGVTI
WYLTNADELQ IKISQGAKPG EGGELPGGKV DEQIARIRHS TPGVGLISPP PHHDIYSIED
MAQLIHDLKN ANRAARISVK LVSEIGVGTI AAGVTKAKTD HLVIAGHDGG TGASPLTSIK
HAGLPWELGL AETHQTLVMN NLRSRVVLQT DGQLKTGRDV AIAALLGAEE FGFATAPLIT
LGCIMMRKCH LNTCPVGIAT QDPELRKKFK GQPEHVVNYL FMVAEELREI MASLGIRTMN
EMVGRVDLLE SNIAINHWKT KGLDLTNILT PAKAVFANTG TYCSMAQDHG LDKALDNQLI
ALAAPTLEKG EKVNIELPVI NINRVVGTML SNEVAKKFGE QMLPDDTINI KLNGSAGQSL
GAFLARGITI TVEGDANDFV GKGLSGGKVV VYPPKNSTFK AEDNIIAGNV NLYGATGGEA
YFRGIVAERF AVRNSGASAV VEGIGDHGCE YMTGGRVVIL GKTGRNFGAG MSGGIAYVWD
KDKDFEKQCN MESFELEPVA DAADIEELKT LISNHLHYTG STVAQQILDN WDASLAQFVK
VMPTDYKRVL AEMAAKAKAQ AVAV
//
