Q9UXR8 (HEM1_METKA) 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:	MK0200

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]

Taxonomic identifier

190192 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus › Methanopyrus kandleri

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. Ref.1
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Enzyme regulation	Inhibited by heavy metal compounds, Zn2+, and heme. Also competitively inhibited by glutamycin. HAMAP-Rule MF_00087
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subunit structure	Homotetramer. Ref.3
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.1. HAMAP-Rule MF_00087 Temperature dependence: Optimum temperature is 90 degrees Celsius.
Mass spectrometry	Molecular mass is 45436±30 Da from positions 1 - 404. Determined by ESI. Ref.1

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing 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 – 404

404

Glutamyl-tRNA reductase HAMAP-Rule MF_00087

PRO_0000114102

Regions

Nucleotide binding

174 – 179

6

NADP Probable

Region

47 – 50

4

Substrate binding HAMAP-Rule MF_00087

Region

99 – 101

3

Substrate binding HAMAP-Rule MF_00087

Sites

Active site

48

1

Nucleophile

Binding site

94

1

Substrate

Binding site

105

1

Substrate

Site

84

1

Important for activity

Experimental info

Mutagenesis

48

1

C → S: Complete loss of activity. Ref.1

Mutagenesis

84

1

H → A: Complete loss of activity. Ref.1

Mutagenesis

84

1

H → N: 30% of wild-type reductase activity. 15% of wild-type esterase activity. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

404

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Turn

11 – 13

3

Helix

16 – 22

7

Helix

29 – 36

8

Beta strand

40 – 47

8

Beta strand

50 – 57

8

Helix

62 – 67

6

Beta strand

74 – 77

4

Helix

78 – 89

12

Turn

90 – 93

4

Beta strand

94 – 96

3

Helix

100 – 116

17

Helix

121 – 140

20

Helix

150 – 162

13

Beta strand

169 – 174

6

Helix

177 – 189

13

Beta strand

192 – 197

6

Helix

201 – 211

11

Helix

218 – 220

3

Helix

221 – 226

6

Beta strand

229 – 233

5

Beta strand

236 – 239

4

Helix

244 – 253

10

Beta strand

260 – 264

5

Helix

275 – 277

3

Beta strand

281 – 285

5

Helix

286 – 301

16

Helix

304 – 350

47

Helix

365 – 382

18

Turn

386 – 390

5

Helix

391 – 402

12

Sequences

	Sequence		Length	Mass (Da)
	Q9UXR8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8B6DBE436EA073B3	FASTA	404	45,444
	10 20 30 40 50 60 MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR VEVYASGARD 70 80 90 100 110 120 RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ EILRQVKKAY DRAARLGTLD 130 140 150 160 170 180 EALKIVFRRA INLGKRAREE TRISEGAVSI GSAAVELAER ELGSLHDKTV LVVGAGEMGK 190 200 210 220 230 240 TVAKSLVDRG VRAVLVANRT YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP 250 260 270 280 290 300 VIHVDDVREA LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR 310 320 330 340 350 360 RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL RRLKTGDPEN 370 380 390 400 VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS ELNG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Methanopyrus kandleri glutamyl-tRNA reductase." Moser J., Lorenz S., Hubschwerlen C., Rompf A., Jahn D. J. Biol. Chem. 274:30679-30685(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, MASS SPECTROMETRY, CATALYTIC MECHANISM, MUTAGENESIS OF CYS-48 AND HIS-84.
[2]	"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[3]	"V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis." Moser J., Schubert W.-D., Beier V., Bringemeier I., Jahn D., Heinz D.W. EMBO J. 20:6583-6590(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, DOMAIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ131561 Genomic DNA. Translation: CAB59204.1.
AE009439 Genomic DNA. Translation: AAM01417.1.

PIR

T45026.

RefSeq

NP_613487.1. NC_003551.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GPJ	X-ray	1.95	A	1-404	[»]

ProteinModelPortal

Q9UXR8.

SMR

Q9UXR8. Positions 1-404.

ModBase

Search...

Protein-protein interaction databases

STRING

190192.MK0200.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAM01417; AAM01417; MK0200.

GeneID

1477503.

KEGG

mka:MK0200.

Phylogenomic databases

eggNOG

COG0373.

HOGENOM

HOG000109651.

KO

K02492.

OMA

MFVLHTC.

Enzyme and pathway databases

BRENDA

1.2.1.70. 3274.

UniPathway

UPA00251; UER00316.

Family and domain databases

Gene3D

1.10.1200.70. 1 hit.
3.40.50.720. 1 hit.

HAMAP

MF_00087. Glu-tRNA_reductase.

InterPro

IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]

Pfam

PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]

PIRSF

PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.

SUPFAM

SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit.
SSF69742. GlutR. 1 hit.

TIGRFAMs

TIGR01035. hemA. 1 hit.

PROSITE

PS00747. GLUTR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UXR8.

Entry information

Entry name

HEM1_METKA

Accession

Primary (citable) accession number: Q9UXR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program