P28462 (HEM1_CHLP8) 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:	Cpar_0738

Organism

Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]

Taxonomic identifier

517417 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum › Chlorobaculum parvum

Protein attributes

Sequence length	426 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). Ref.2
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. Ref.2
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 Was shown to bind heme, but the precise role of heme is unclear. HAMAP-Rule MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete 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 – 426	426	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_0000114009
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity
	Site	99	1	Important for activity By similarity
Experimental info
	Sequence conflict	144 – 145	2	TA → SP in AAC61856. Ref.1
	Sequence conflict	144 – 145	2	TA → SP in AAA23112. Ref.1
	Sequence conflict	191 – 223	33	GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAC61856. Ref.1
	Sequence conflict	191 – 223	33	GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAA23112. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P28462 [UniParc]. Last modified October 14, 2008. Version 3. Checksum: D169328D709EF697	FASTA	426	48,142
	10 20 30 40 50 60 MNIISVGVNH KTAPIEIRER IALSEVQNKE FVTDLVSSGL ASEAMVVSTC NRTELYVVPG 70 80 90 100 110 120 MPEVNCDYLK DYIISYKDAR NAVRPEHFFN RFYCGTARHL FEVSSAIDSL VLGEGQILGQ 130 140 150 160 170 180 VKDAYRIAAE VGTAGILLTR LCHTAFSVAK KVKTRTKLME GAVSVSYAAV ELAQKIFSNL 190 200 210 220 230 240 SMKKVLLIGA GETGELAAKH MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH 250 260 270 280 290 300 LHEFDIIITA VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 310 320 330 340 350 360 IDALKHIIDK NLERRRAELP KVKSIIDEEL IGFGQWINTL KVRPTIVDLQ SKFIEIKEKE 370 380 390 400 410 420 LERYRHKVSE EELKRMEHLT DRILKKILHH PIKMLKAPVD TADNIPSKVN LVRNIFDLEE PNQSLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the Chlorobium vibrioforme hemA gene." Majumdar D., Avissar Y.J., Wyche J.H., Beale S.I. Arch. Microbiol. 156:281-289(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit." Srivastava A., Beale S.I. J. Bacteriol. 187:4444-4450(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS, FUNCTION, HEME BINDING, SUBUNIT.
[3]	"Complete sequence of Chlorobaculum parvum NCIB 8327." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. , Overmann J., Bryant D.A., Richardson P. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCIB 8327.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M96364 Genomic DNA. Translation: AAA23112.1. AF080069 Genomic DNA. Translation: AAC61856.1. CP001099 Genomic DNA. Translation: ACF11155.1.
PIR	A48359.
RefSeq	YP_001998355.1. NC_011027.1.
3D structure databases
ProteinModelPortal	P28462.
ModBase	Search...
Protein-protein interaction databases
STRING	517417.Cpar_0738.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACF11155; ACF11155; Cpar_0738.
GeneID	6419665.
KEGG	cpc:Cpar_0738.
PATRIC	21364734. VBIChlPar72705_0737.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109651.
KO	K02492.
OMA	YLYNLDD.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	CPAR517417:GH95-766-MONOMER.
BRENDA	1.2.1.70. 1348.
UniPathway	UPA00251; UER00316.
Family and domain databases
Gene3D	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...

Entry information

Entry name

HEM1_CHLP8

Accession

Primary (citable) accession number: P28462
Secondary accession number(s): B3QMK2, O87494

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program