hemA

Functionⁱ

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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.UniRule annotation

Catalytic activityⁱ

L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayⁱ: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Glutamyl-tRNA reductase (hemA)
Glutamate-1-semialdehyde 2,1-aminomutase (hemL)

This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	50	NucleophileUniRule annotation	1
Siteⁱ	97	Important for activityUniRule annotation	1
Binding siteⁱ	107	SubstrateUniRule annotation	1
Binding siteⁱ	118	SubstrateUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	187 – 192	NADPUniRule annotation		6

GO - Molecular functionⁱ

glutamyl-tRNA reductase activity Source: UniProtKB-EC
NADP binding Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Porphyrin biosynthesis
Ligand	NADP

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00316.

UniPathwayⁱ

UPA00251; UER00316.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation) Short name: GluTRUniRule annotation
Gene namesⁱ	Name:hemAUniRule annotation Ordered Locus Names:Ping_1606
Organismⁱ	Psychromonas ingrahamii (strain 37)
Taxonomic identifierⁱ	357804 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Psychromonadaceae › Psychromonas › Psychromonas ingrahamii
Proteomesⁱ	UP000000639 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_1000004678	1 – 419	Glutamyl-tRNA reductaseAdd BLAST		419

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGⁱ	357804.Ping_1606.

STRINGⁱ

357804.Ping_1606.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	A1SV88.
SMRⁱ	A1SV88.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	49 – 52	Substrate bindingUniRule annotation		4
Regionⁱ	112 – 114	Substrate bindingUniRule annotation		3

Domainⁱ

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.UniRule annotation

Sequence similaritiesⁱ

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C7E. Bacteria. COG0373. LUCA.
HOGENOMⁱ	HOG000109650.
KEGG Orthology (KO) More...KOⁱ	K02492.
OMAⁱ	FAFKCAA.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H05DA.

Family and domain databases

HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	View protein in InterPro IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR018214. GluRdtase_CS. IPR016040. NAD(P)-bd_dom. IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit.
PIRSFⁱ	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMⁱ	SSF51735. SSF51735. 1 hit. SSF69075. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit.
TIGRFAMsⁱ	TIGR01035. hemA. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00747. GLUTR. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

A1SV88-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPLFALGINH QTASVALREK VAFSADLLLD AYQALLAQPT VLEAVIVSTC 
        60         70         80         90        100
NRTEIYCHLK QDNCDEVIKW LCSFHQIEDH KLRPSLYCYS EYQAIQHLFR 
       110        120        130        140        150
VSCGLDSLVL GEPQILGQIK QAFATAKQAK GVDKIVQKWF QHTFTVAKRV 
       160        170        180        190        200
RTETQIGANA ISVAFAAVCL AKQIFSDLSQ SRVLLIGAGE TIELVGKYLI 
       210        220        230        240        250
EHQVPNITIA NRTLSRAMAL VEQFDAQAIT LGEIPNHLAQ ADIIISSTAS 
       260        270        280        290        300
PLPIIGKGMV ERALKARRNR PMLFIDIAVP RDIEAEVSEL RDIYLYSVDD 
       310        320        330        340        350
LQGIIEENKQ ARQVAALEAE KIIDGCIVDF ISWIESLKAV ESIRTYRQNS 
       360        370        380        390        400
EQLRDDLLNR ASAALQNGEE AENVLKELAF KLTNKLIHHP SLALNETARS 
       410 
GNDDELILLR NALGLSKKD

Length:419

Mass (Da):46,623

Last modified:February 6, 2007 - v1

Checksum:ⁱAD814071E15F5CFB

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000510 Genomic DNA. Translation: ABM03403.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_011769963.1. NC_008709.1.

Genome annotation databases

EnsemblBacteriaⁱ	ABM03403; ABM03403; Ping_1606.
KEGGⁱ	pin:Ping_1606.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000510 Genomic DNA. Translation: ABM03403.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_011769963.1. NC_008709.1.

3D structure databases

ProteinModelPortalⁱ	A1SV88.
SMRⁱ	A1SV88.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	357804.Ping_1606.

STRINGⁱ

357804.Ping_1606.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ABM03403; ABM03403; Ping_1606.
KEGGⁱ	pin:Ping_1606.

Phylogenomic databases

eggNOGⁱ	ENOG4105C7E. Bacteria. COG0373. LUCA.
HOGENOMⁱ	HOG000109650.
KEGG Orthology (KO) More...KOⁱ	K02492.
OMAⁱ	FAFKCAA.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H05DA.

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00316.

UniPathwayⁱ

UPA00251; UER00316.

Family and domain databases

HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	View protein in InterPro IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR018214. GluRdtase_CS. IPR016040. NAD(P)-bd_dom. IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit.
PIRSFⁱ	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMⁱ	SSF51735. SSF51735. 1 hit. SSF69075. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit.
TIGRFAMsⁱ	TIGR01035. hemA. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00747. GLUTR. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HEM1_PSYIN
Accessionⁱ	A1SV88Primary (citable) accession number: A1SV88
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
	Last sequence update:	February 6, 2007
	Last modified:	June 7, 2017
	This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

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Supporting data

UniProtKB - A1SV88 (HEM1_PSYIN)

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Glutamyl-tRNA reductase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protoporphyrin-IX biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: protoporphyrin-IX biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ