Reviewed, UniProtKB/Swiss-Prot B2ULP2 (HEM1_AKKM8)

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:	Amuc_0091

Organism

Akkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]

Taxonomic identifier

349741 [NCBI]

Taxonomic lineage

Bacteria › Verrucomicrobia › Verrucomicrobiae › Verrucomicrobiales › Verrucomicrobiaceae › Akkermansia

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP 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.
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.
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 340	340	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000093112
Regions
	Nucleotide binding	188 – 193	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	113 – 115	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Site	98	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2ULP2-1 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: 27D3C2F5FF5D3612	FASTA	340	37,606
	10 20 30 40 50 60 MRMVCLGLNH RTAPVEIRER FAVPSHKLRE EGQRIRSLPG VDQCVVLSTC NRMEIYYWSN 70 80 90 100 110 120 APENAQEHIL SHFLGDGRGE LDMASYFYSH QGEDALGHLC RVLSGLDSMV LGETEIFGQV 130 140 150 160 170 180 KTAYQTALDA GVTAACANKT FQKAFTIGKK VRTESQIHAG ATSVGSVAVE LAEQIFGDLS 190 200 210 220 230 240 GTRVLILGAG EMSRVTGRAL HARGAEGIYV ANRSFDRAVE LAGMIGGQAI RYDVWGNYLR 250 260 270 280 290 300 DIDVVVAATA APHCIITRET LLPLRASRKY RSLFLIDISV PRNISPDVAD IDEVYLYDID 310 320 330 340 TLTQLADEAK RSRKQEVSRC EAIIRDSISR YFPDSALYDQ

References

[1]

"Complete sequence of Akkermansia muciniphila ATCC BAA-835." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P. Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001071 Genomic DNA. Translation: ACD03936.1.
RefSeq	YP_001876717.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6274993.
GenomeReviews	Gene locus Amuc_0091 in contig CP001071_GR.
KEGG	amu:Amuc_0091.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	GPILNRL.
Family and domain databases
HAMAP	MF_00087. [Tree]
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_AKKM8

Accession

Primary (citable) accession number: B2ULP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 1, 2008
Last modified:	November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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