GLTD_AZOBR
ID GLTD_AZOBR Reviewed; 482 AA.
AC Q05756; Q9EXL4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glutamate synthase [NADPH] small chain;
DE EC=1.4.1.13;
DE AltName: Full=Glutamate synthase subunit beta;
DE Short=GLTS beta chain;
DE AltName: Full=NADPH-GOGAT;
GN Name=gltD;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24; 183-204
RP AND 328-344.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=8428988; DOI=10.1016/s0021-9258(18)53664-4;
RA Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B.,
RA Zanetti G.;
RT "Glutamate synthase genes of the diazotroph Azospirillum brasilense.
RT Cloning, sequencing, and analysis of functional domains.";
RL J. Biol. Chem. 268:3099-3106(1993).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Vanoni M.A., Verzotti E., Morandi P., Curti B.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2198943; DOI=10.1016/0167-4838(90)90273-i;
RA Vanoni M.A., Negri A., Zanetti G., Ronchi S., Curti B.;
RT "Structural studies on the subunits of glutamate synthase from Azospirillum
RT brasilense.";
RL Biochim. Biophys. Acta 1039:374-377(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-8.
RC STRAIN=Sp6;
RX PubMed=8001567; DOI=10.1111/j.1432-1033.1994.tb20075.x;
RA Vanoni M.A., Mazzoni A., Fumagalli P., Negri A., Zanetti G., Curti B.;
RT "Interdomain loops and conformational changes of glutamate synthase as
RT detected by limited proteolysis.";
RL Eur. J. Biochem. 226:505-515(1994).
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
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.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC -!- SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting of a
CC large and a small subunit.
CC -!- MISCELLANEOUS: Glutamine binds to the large subunit and transfers the
CC amido group to 2-oxo-glutamate that apparently binds to the small
CC subunit.
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DR EMBL; AF192408; AAG38999.1; -; Genomic_DNA.
DR PIR; A46602; A46602.
DR RefSeq; WP_035677957.1; NZ_VITX01000012.1.
DR PDB; 2VDC; EM; 9.50 A; G/H/I/J/K/L=27-482.
DR PDB; 6S6S; EM; 3.90 A; E/F/G/H=1-482.
DR PDB; 6S6T; EM; 4.10 A; E/F/G=1-482.
DR PDB; 6S6U; EM; 3.50 A; G/H/I/J=1-482.
DR PDB; 6S6X; EM; 3.50 A; G/H/I/J/K/L=1-482.
DR PDBsum; 2VDC; -.
DR PDBsum; 6S6S; -.
DR PDBsum; 6S6T; -.
DR PDBsum; 6S6U; -.
DR PDBsum; 6S6X; -.
DR AlphaFoldDB; Q05756; -.
DR SASBDB; Q05756; -.
DR SMR; Q05756; -.
DR PRIDE; Q05756; -.
DR GeneID; 56449275; -.
DR KEGG; ag:AAG38999; -.
DR OrthoDB; 671513at2; -.
DR BioCyc; MetaCyc:MON-13080; -.
DR BRENDA; 1.4.1.13; 611.
DR SABIO-RK; Q05756; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR EvolutionaryTrace; Q05756; -.
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 3D-structure; 4Fe-4S; Amino-acid biosynthesis; Direct protein sequencing;
KW Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8001567,
FT ECO:0000269|PubMed:8428988"
FT CHAIN 2..482
FT /note="Glutamate synthase [NADPH] small chain"
FT /id="PRO_0000170799"
FT DOMAIN 39..72
FT /note="4Fe-4S ferredoxin-type"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:6S6X"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 348..370
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 381..392
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6S6U"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:6S6U"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:6S6U"
FT HELIX 451..474
FT /evidence="ECO:0007829|PDB:6S6U"
SQ SEQUENCE 482 AA; 52358 MW; 8224C1B4EAAFCB25 CRC64;
MANQRMLGFV HTAQRMPDKR PAAERRQDFA EIYARFSDER ANEQANRCSQ CGVPFCQVHC
PVSNNIPDWL KLTSEGRLEE AYEVSQATNN FPEICGRICP QDRLCEGNCV IEQSTHGAVT
IGSVEKYIND TAWDQGWVKP RTPSRELGLS VGVIGAGPAG LAAAEELRAK GYEVHVYDRY
DRMGGLLVYG IPGFKLEKSV VERRVKLLAD AGVIYHPNFE VGRDASLPEL RRKHVAVLVA
TGVYKARDIK APGSGLGNIV AALDYLTTSN KVSLGDTVEA YENGSLNAAG KHVVVLGGGD
TAMDCVRTAI RQGATSVKCL YRRDRKNMPG SQREVAHAEE EGVEFIWQAA PEGFTGDTVV
TGVRAVRIHL GVADATGRQT PQVIEGSEFT VQADLVIKAL GFEPEDLPNA FDEPELKVTR
WGTLLVDHRT KMTNMDGVFA AGDIVRGASL VVWAIRDGRD AAEGIHAYAK AKAEAPVAVA
AE
