Reviewed, UniProtKB/Swiss-Prot A4XK04 (HEM1_CALS8)

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:	Csac_1649

Organism

Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]

Taxonomic identifier

351627 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	394 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
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 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 – 394	394	Glutamyl-tRNA reductase		PRO_1000004603
Regions
	Nucleotide binding	175 – 180	6	NADP By similarity
	Region	45 – 48	4	Substrate binding By similarity
	Region	104 – 106	3	Substrate binding By similarity
Sites
	Active site	46	1	Nucleophile By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity
	Site	89	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4XK04-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 375F79C2B3BD64E1	FASTA	394	46,005
	10 20 30 40 50 60 MLWVIGINHK VEVDIRQKFS LTKTKLQEKL ISLKKLADEV IILSTCNRTE IYFFSEEYVD 70 80 90 100 110 120 IEKIFTELDW DRRYMPLFYI YKDKDCIKHL FEVVCGFDSL LIGEEQIVAQ VKEAKDIAKQ 130 140 150 160 170 180 VGGKNPVLER LFEVALKCSK EFRTKARLNE HPITIASVVG KVLKESNIRK IAIIGLGNIG 190 200 210 220 230 240 FLFCNYFKNS DVDKVFLIGR KNERIDQFVK LYPGKFEYSD KKDAISEAQC LICSTSAPHA 250 260 270 280 290 300 VVHKDDIPDG KNLLIFDLAV PRDVDVEVYK LPNVKVIDID QVHKMDATSR EIRISKMQEN 310 320 330 340 350 360 YNIIEKYIDE FIEWLGFRQY RNLIIEVKRH AEQLCKAQVK YLKNVDSRER EEVERLLIRM 370 380 390 ANLYIDRAIE VLREAHKEGS GEICSNLIKR IFLK

References

[1]

"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000679 Genomic DNA. Translation: ABP67239.1.
RefSeq	YP_001180430.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5088968.
GenomeReviews	Gene locus Csac_1649 in contig CP000679_GR.
KEGG	csc:Csac_1649.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd. IPR006151. Shikm_DHase/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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_CALS8

Accession

Primary (citable) accession number: A4XK04

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 29, 2007
Last modified:	November 25, 2008
This is version 14 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)