Q8R687 (HEM1_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase
Short name=GluTR
EC=1.2.1.70

Gene names

Name:	hemA
Ordered Locus Names:	FN0646

Organism

Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]

Taxonomic identifier

190304 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Fusobacteria › Fusobacteriia › Fusobacteriales › Fusobacteriaceae › Fusobacterium › Fusobacterium nucleatum › Fusobacterium nucleatum subsp. nucleatum

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087
Subunit structure	Homodimer By similarity.
Domain	Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087
Miscellaneous	During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity. HAMAP-Rule MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.
Caution	Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_0000114027
Regions
	Nucleotide binding	179 – 184	6	NADP By similarity
	Region	51 – 54	4	Substrate binding By similarity
	Region	104 – 106	3	Substrate binding By similarity
Sites
	Active site	52	1	Nucleophile By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8R687 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 675E1B115629E9E2	FASTA	329	38,592
	10 20 30 40 50 60 MLDLENIIVI GVSHENLSLL ERENFMRTRP KYIIERLYTE KKINAYINLS TCLRTEFYIE 70 80 90 100 110 120 LNSNIKAKEI KNLFSVDMIV KSRVEAIEYL FKVGCGFYSV IKGEDQILAQ VKGAYAEALE 130 140 150 160 170 180 NEHSSKFLNI IFNKSIELGK KFRTKSMIAH NALSLEAISL KFIKSKFPNI EDKNIFILGI 190 200 210 220 230 240 GELAQDILTL LTKEQLKNIY IANRTYHKAE QIKKEFDIVN IVDYREKYPK MIEADVIISA 250 260 270 280 290 300 TSAPHIVVEY DKFVAQMKEN KDYLFIDLAV PRDVDERLAN FKNIEIYNLD DIWEVYHLNS 310 320 MNRDKLLEDY SYLIDEQMEK LIKTLNYYK

References

[1]

"Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum strain ATCC 25586." Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N. , D'Souza M., Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C., Overbeek R. J. Bacteriol. 184:2005-2018(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009951 Genomic DNA. Translation: AAL94842.1.
RefSeq	NP_603543.1. NC_003454.1.
3D structure databases
ProteinModelPortal	Q8R687.
ModBase	Search...
Protein-protein interaction databases
STRING	190304.FN0646.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL94842; AAL94842; FN0646.
GeneID	993220.
KEGG	fnu:FN0646.
PATRIC	21951055. VBIFusNuc122357_1210.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109108.
KO	K02492.
OMA	HTCNRVE.
ProtClustDB	CLSK2518845.
Enzyme and pathway databases
UniPathway	UPA00251; UER00316.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase. Divergent sequence.
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. Pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Pfam	PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
SUPFAM	SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_FUSNN

Accession

Primary (citable) accession number: Q8R687

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program