Reviewed, UniProtKB/Swiss-Prot Q05756 (GLTD_AZOBR)

Names and origin

Protein names

Recommended name:
    Glutamate synthase [NADPH] small chain
    EC=1.4.1.13
Alternative name(s):
    Glutamate synthase subunit beta
      Short name=GLTS beta chain
    NADPH-GOGAT

Gene names

Name:

gltD

Organism

Azospirillum brasilense

Taxonomic identifier

192 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Azospirillum

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH.
Cofactor	Binds 1 4Fe-4S cluster.
Pathway	Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADPH route): step 1/1. Energy metabolism; nitrogen metabolism.
Subunit structure	Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.
Miscellaneous	Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit.
Sequence similarities	Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Glutamate biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro glutamate synthase (NADPH) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.4
	Chain	2 – 482	481	Glutamate synthase [NADPH] small chain		PRO_0000170799
Regions
	Domain	39 – 72	34	4Fe-4S ferredoxin-type
Sites
	Metal binding	95	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	99	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	105	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	109	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q05756-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8224C1B4EAAFCB25	FASTA	482	52,358
	10 20 30 40 50 60 MANQRMLGFV HTAQRMPDKR PAAERRQDFA EIYARFSDER ANEQANRCSQ CGVPFCQVHC 70 80 90 100 110 120 PVSNNIPDWL KLTSEGRLEE AYEVSQATNN FPEICGRICP QDRLCEGNCV IEQSTHGAVT 130 140 150 160 170 180 IGSVEKYIND TAWDQGWVKP RTPSRELGLS VGVIGAGPAG LAAAEELRAK GYEVHVYDRY 190 200 210 220 230 240 DRMGGLLVYG IPGFKLEKSV VERRVKLLAD AGVIYHPNFE VGRDASLPEL RRKHVAVLVA 250 260 270 280 290 300 TGVYKARDIK APGSGLGNIV AALDYLTTSN KVSLGDTVEA YENGSLNAAG KHVVVLGGGD 310 320 330 340 350 360 TAMDCVRTAI RQGATSVKCL YRRDRKNMPG SQREVAHAEE EGVEFIWQAA PEGFTGDTVV 370 380 390 400 410 420 TGVRAVRIHL GVADATGRQT PQVIEGSEFT VQADLVIKAL GFEPEDLPNA FDEPELKVTR 430 440 450 460 470 480 WGTLLVDHRT KMTNMDGVFA AGDIVRGASL VVWAIRDGRD AAEGIHAYAK AKAEAPVAVA AE

References

[1]	"Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing, and analysis of functional domains." Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B., Zanetti G. J. Biol. Chem. 268:3099-3106(1993) [PubMed: 8428988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24; 183-204 AND 328-344. Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
[2]	Vanoni M.A., Verzotti E., Morandi P., Curti B. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]	"Structural studies on the subunits of glutamate synthase from Azospirillum brasilense." Vanoni M.A., Negri A., Zanetti G., Ronchi S., Curti B. Biochim. Biophys. Acta 1039:374-377(1990) [PubMed: 2198943] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[4]	"Interdomain loops and conformational changes of glutamate synthase as detected by limited proteolysis." Vanoni M.A., Mazzoni A., Fumagalli P., Negri A., Zanetti G., Curti B. Eur. J. Biochem. 226:505-515(1994) [PubMed: 8001567] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Strain: Sp6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF192408 Genomic DNA. Translation: AAG38999.1.

PIR

A46602.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VDC	electron microscopy	9.50	G/H/I/J/K/L	27-482	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13080.

BRENDA

1.4.1.13. 1315.

Family and domain databases

InterPro

IPR000759. Adrndx_reductase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR012285. Fum_reductase_C.
IPR006006. Glut_synth_sub2.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00419. ADXRDTASE.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01318. gltD_gamma_fam. 1 hit.

PROSITE

PS51379. 4FE4S_FER_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLTD_AZOBR

Accession

Primary (citable) accession number: Q05756
Secondary accession number(s): Q9EXL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)