Reviewed, UniProtKB/Swiss-Prot A9KSC2 (HEM12_CLOPH)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 2
      Short name=GluTR 2
    EC=1.2.1.70

Gene names

Name:	hemA2
Ordered Locus Names:	Cphy_1784

Organism

Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]

Taxonomic identifier

357809 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	413 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 – 413	413	Glutamyl-tRNA reductase 2 HAMAP MF_00087		PRO_0000335024
Regions
	Nucleotide binding	186 – 191	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	111 – 113	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9KSC2-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 98276B1B10DCAAFA	FASTA	413	47,150
	10 20 30 40 50 60 MNISMVGIDY NTASIEDREH FTLTSDKQLE IAKIIKETYH ASGCIILSTC NRTEIWFSEL 70 80 90 100 110 120 GTSEAECFHQ LVLGENAKET MRSICVCRQG DEAVTYLMEL GCGIHSQIFG EDQILTQLKQ 130 140 150 160 170 180 ALQQARDYQY VDSVLECLFR TAITAAKKVK TSIQIAKGNT SLPQTIVEQL EKEQGDLLGK 190 200 210 220 230 240 SCLVIGNGEM GRLMTEKLLE KKCKVWMTLR QYKKSKAIIP EGSGVVLYDE RYEHIAVMDY 250 260 270 280 290 300 IFSATKSHHF TINKSMFENI RLKGKTYCLI DLAIPRDIEP SVEELSDVTV YNMDYFCQEV 310 320 330 340 350 360 NDREKELEET RELLSEYVNE FKQWYQFRNL VSTVDDISNI VSDITDAKLT KVYKSIDLSR 370 380 390 400 410 EQQELLQSNV QMAAKKAVSK IIFGLRDVLQ IDQCEEVLQA LEQSAMNCTD SVK

References

[1]

"Complete genome sequence of Clostridium phytofermentans ISDg." Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000885 Genomic DNA. Translation: ABX42154.1.
RefSeq	YP_001558893.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5741457.
GenomeReviews	Gene locus Cphy_1784 in contig CP000885_GR.
KEGG	cpy:Cphy_1784.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A9KSC2. EVRPEHF.
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]
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM12_CLOPH

Accession

Primary (citable) accession number: A9KSC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	June 16, 2009
This is version 15 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)