GLTD_HALED
ID GLTD_HALED Reviewed; 472 AA.
AC E1V8I0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Glutamate synthase [NADPH] small chain {ECO:0000250|UniProtKB:P09832};
DE EC=1.4.1.13 {ECO:0000269|PubMed:28081159};
DE AltName: Full=GOGAT {ECO:0000303|PubMed:28081159};
DE AltName: Full=Glutamate synthase subunit beta {ECO:0000250|UniProtKB:P09832};
DE Short=GLTS beta chain {ECO:0000250|UniProtKB:P09832};
GN Name=gltD {ECO:0000303|PubMed:28081159};
GN OrderedLocusNames=HELO_3752 {ECO:0000312|EMBL:CBV43636.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA Kunte H.J.;
RT "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT study for integrative systems biology.";
RL PLoS ONE 12:E0168818-E0168818(2017).
CC -!- FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate
CC into two molecules of L-glutamate. {ECO:0000269|PubMed:28081159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000269|PubMed:28081159};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1. {ECO:0000250|UniProtKB:P09832}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000250|UniProtKB:P09832}.
CC -!- INDUCTION: Up-regulated at high salt concentration.
CC {ECO:0000269|PubMed:28081159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN869568; CBV43636.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V8I0; -.
DR SMR; E1V8I0; -.
DR STRING; 768066.HELO_3752; -.
DR EnsemblBacteria; CBV43636; CBV43636; HELO_3752.
DR KEGG; hel:HELO_3752; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_6; -.
DR OMA; DCVGTAH; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR42783:SF1; PTHR42783:SF1; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR TIGRFAMs; TIGR01318; gltD_gamma_fam; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Glutamate biosynthesis; Iron; Iron-sulfur;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..472
FT /note="Glutamate synthase [NADPH] small chain"
FT /id="PRO_0000439540"
FT DOMAIN 41..72
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 472 AA; 51995 MW; 24A9D53E87AE5413 CRC64;
MANRLNNDFQ FIDVGRQDPE KKPARTRAKQ FAEIYEPYKP QDAAAQAHRC LHCGNPYCEW
KCPVHNYIPN WLQLVSEGNI LEAAELSHRT NSLPEVCGRV CPQDRLCEGD CTLNDGFGAV
TIGSVEKYIT DTAFAMGWRP DMSKVTWTDK KVAIIGAGPA GLGCADILVR NGVKPVVFDK
YPEIGGLLTF GIPEFKLEKT VMERRRAVFE EMGVEFCLGV EIGRDMPFEQ LLEEYDAVFL
GMGTYKYMEG GFPGEDLPGV HKALDYLVAN VNHCLGFETD PADYVSLEGQ RVVVLGGGDT
AMDCNRTAIR QGAASVTCAY RRDEDNMPGS RKEVANAREE GVDFLFNRQP VAVIGEDRVE
GIKVVRTRLG EPDENGRQRP EVVPGSEEVV PADAVVIAFG FQPSPAPWFE TVGIELDEKG
RVKAPEEGAY AFQTTNEKIF AGGDMVRGSD LVVTAVFEGR QAGEGILDYL DV
