Reviewed, UniProtKB/Swiss-Prot Q03460 (GLSN_MEDSA)

Names and origin

Protein names	Recommended name:     Glutamate synthase [NADH], amyloplastic     EC=1.4.1.14 Alternative name(s):     NADH-GOGAT
Organism	Medicago sativa (Alfalfa)
Taxonomic identifier	3879 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	2194 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 + NAD+ = L-glutamine + 2-oxoglutarate + NADH.
Cofactor	Binds 1 3Fe-4S cluster. FAD. FMN.
Pathway	Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADH route): step 1/1. Energy metabolism; nitrogen metabolism.
Subunit structure	Monomer.
Subcellular location	Plastid › amyloplast Potential.
Tissue specificity	Root nodules.
Sequence similarities	Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Glutamate biosynthesis
Cellular component	Amyloplast Plastid
Domain	Glutamine amidotransferase Transit peptide
Ligand	3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro glutamate synthase (NADH) 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
	Transit peptide	1 – 101	101	Amyloplast Ref.1
	Chain	102 – 2194	2093	Glutamate synthase [NADH], amyloplastic		PRO_0000011617
Regions
	Domain	102 – 503	402	Glutamine amidotransferase type-2
	Nucleotide binding	1193 – 1250	58	FMN By similarity
	Nucleotide binding	1974 – 1988	15	NAD Potential
Sites
	Active site	102	1	For GATase activity By similarity
	Metal binding	1246	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1252	1	Iron-sulfur (3Fe-4S) By similarity
	Metal binding	1257	1	Iron-sulfur (3Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03460-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 370A1B0F178367C4	FASTA	2,194	240,374
	10 20 30 40 50 60 MSNSLSLTFT ALNNPQINAI SNPNARLRPL ARVTRCSATC VERKRWLGTK LRSGGGLERI 70 80 90 100 110 120 QLWESGGLGR LPKLRVAVKS SFSAVPDKPM GLYDPAFDKD SCGVGFVAEL NGQSSRKTVT 130 140 150 160 170 180 DALEMLVRMT HRGACGCEAN TGDGAGILVA LPHGFYQEVV DFQLPPQGNY AVGMFFLPKS 190 200 210 220 230 240 DSRRKESKNI FTKVAESLGH KVLGWRSVPT DNTGLGKSAQ LTEPVIEQVF LTPSSDSKVD 250 260 270 280 290 300 LEKQMYILRK LSMVSITSAL NLQSDGITDF YICSLSSRTV IYKGQLTPAQ LGEYYYADLG 310 320 330 340 350 360 NERFTSYMAL IHSRFSTNTF PSWDRAQPFR VLGHNGEINT LRGNVNWIKA REGLLKCKEL 370 380 390 400 410 420 GLSENDLKKF LPIVDANSSD SGCFDGVLEF LLHSGKSLPE AVMMMIPEAW QNDKNMDPQR 430 440 450 460 470 480 KAFYEYYSAL MEPWDGPALI SFTDGHYLGA TLDRNGLRPG RFYVTHSGRV IMASEVGVVD 490 500 510 520 530 540 IPPEDVCRKG RLNPGMMLLV DFEKQIVVND DALKEQYSLA RPYGDWLEKQ KIELKDIIDS 550 560 570 580 590 600 VHESDIVPPT ISGVPPLSND DVDMENMGIQ GLLAPLKAFG YSVESLEILL LPMAKDGVEA 610 620 630 640 650 660 LGSMGNDTPL AVMSNREKLT FEYFKQMFAQ VTNPPIDPIR EKIVTSMRCM VGPEGDLTET 670 680 690 700 710 720 TEEQCHRLSL KGPLLSTKEM EAIKKMNYRG WRSKVIDITY SKERGTKGLE EALDRICTEA 730 740 750 760 770 780 HNAISEGYTT LVLSDRAFSK KHVAVSSLLA VGAVHQHLVK TLERTRVALM VESAEPREVH 790 800 810 820 830 840 HFCTLVGFGA DAICPYLAIE AIWRLQVDGK IPPKASGDFN SKDELVKKYF KASTYGMMKV 850 860 870 880 890 900 LAKMGISTLA SYKGAQIFEA LGLSSEVIEK CFAGTPSRVE GATFEMLAQD ALHLHELAFP 910 920 930 940 950 960 SRIFSPGSAE AVALPNPGDY HWRKGGEVHL NDPLAIAKLQ EAARTNSVDA YKQYSKTIHE 970 980 990 1000 1010 1020 LNKACNLRGL LKFKDAASKV PISEVEPASE IVKRFCTGAM SYGSISLEAH TALATAMNTI 1030 1040 1050 1060 1070 1080 GGKSNTGEGG EQPSRMEPLA DGSRNPKRSA IKQVASGRFG VSSYYLTNAD ELQIKMAQGA 1090 1100 1110 1120 1130 1140 KPGEGGELPG HKVIGDIAIT RNSTAGVGLI SPPPHHDIYS IEDLAQLIHD LKNANPAARI 1150 1160 1170 1180 1190 1200 SVKLVSEAGV GVIASGVVKG HAEHVLISGH DGGTGASRWT GIKSAGLPWE LGLAETHQTL 1210 1220 1230 1240 1250 1260 VANDLRGRTT LQTDGQLKTG RDVAIAALLG AEEYGFSTAP LITLGCIMMR KCHKNTCPVG 1270 1280 1290 1300 1310 1320 IATQDPVLRE KFAGEPEHVI NFFFMVAEEM REIMSQLGFR TVNEMVGRSD MLEVDKEVVK 1330 1340 1350 1360 1370 1380 GNAKLENIDL SLLLRPAAEL RPEAAQYCVQ KQDHGLDMAL DNKLISLSNA ALEKGLPVYI 1390 1400 1410 1420 1430 1440 ETPICNTNRA VGTMLSHEVT KRYNLAGLPA DTIHIQFTGS AGQSFGAFLC PGITLELEGD 1450 1460 1470 1480 1490 1500 SNDYIGKGLS GGKVVVYPPK GSNFDPKDNI LIGNVALYGA TRGEAYFNGM AAERFCVRNS 1510 1520 1530 1540 1550 1560 GALAVVEGVG DHGCEYMTGG TVVVLGKTGR NFAAGMSGGI AYVLDVDGTF QSRCNLELVD 1570 1580 1590 1600 1610 1620 LDKVEEEEDI ITLRMLIQQH QRHTNSLLAK EVLVDFENLL PKFVKVFPRE YKRVLASMKS 1630 1640 1650 1660 1670 1680 DAASKDAVER AAEDVDEQDD EAQAVEKDAF EELKKLATAS LNEKPSEAPK RPSQVTDAVK 1690 1700 1710 1720 1730 1740 HRGFVAYERE GVQYRDPNVR LNDWNEVMME TKPGPLLKTQ SARCMDCGTP FCHQENSGCP 1750 1760 1770 1780 1790 1800 LGNKIPEFNE LVYQNRWQEA LERLLETNNF PEFTGRVCPA PCEGSCVLGI IENPVSIKNI 1810 1820 1830 1840 1850 1860 ECAIIDKAFE EGWMIPRPPV KRTGKRVAIV GSGPSGLAAA DQLNKMGHIV TVFERADRIG 1870 1880 1890 1900 1910 1920 GLMMYGVPNM KTDKVDIVQR RVNLMAEEGI NFVVNANIGL DPLYSLERLR EENDAIVLAV 1930 1940 1950 1960 1970 1980 GATKPRDLPV PGRELSGVHF AMEFLHANTK SLLDSNLQDG NYISAKGKKV VVIGGGDTGT 1990 2000 2010 2020 2030 2040 DCIGTSIRHG CTAVVNLELL PQPPPTRAPG NPWPQWPRIF RVDYGHQEAE TKFGKDPRTY 2050 2060 2070 2080 2090 2100 EVLTKRFVGD ENGVVKGLEV VRVCWEKDET GKFQFKEIEG SEEIIEADLV LLAMGFLGPE 2110 2120 2130 2140 2150 2160 ATIAEKLGVE RDNRSNFKAD YGRFSTSVDG VFAAGDCRRG QSLVVWAISE GRQAAAQVDS 2170 2180 2190 YLTNEDHGID GNQDEFVKRQ QDLNKKHSKH TVMT

References

[1]	"Molecular characterization of NADH-dependent glutamate synthase from alfalfa nodules." Gregerson R.G., Miller S.S., Twary S.N., Gantt J.S., Vance C.P. Plant Cell 5:215-226(1993) [PubMed: 8453303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-114.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L01660 mRNA. Translation: AAB46617.1.
PIR	JQ1977.
3D structure databases
HSSP	HSSP built from PDB template 1LM1 based on UniProtKB P55038.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.4.1.14. 815.
Family and domain databases
InterPro	IPR000759. Adrndx_reductase. IPR013785. Aldolase_TIM. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR012285. Fum_reductase_C. IPR000583. GATase_2. IPR017932. GATase_II. IPR002932. Glu_synth_centr_C. IPR006982. Glu_synth_centr_N. IPR002489. Glu_synthase_C. IPR006005. Glut_synth_sub1. IPR012220. GOGAT_euk. IPR016040. NAD(P)-bd_dom. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 2 hits. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit. G3DSA:2.160.20.60. Glu_synthase_C. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. PF04898. Glu_syn_central. 1 hit. PF01645. Glu_synthase. 1 hit. PF01493. GXGXG. 1 hit. PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PIRSF	PIRSF000187. GOGAT. 1 hit.
PRINTS	PR00419. ADXRDTASE.
TIGRFAMs	TIGR01317. GOGAT_sm_gam. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLSN_MEDSA

Accession

Primary (citable) accession number: Q03460

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)