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Q59292 (HEMA_CLOJO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probale multifunctional siroheme biosynthesis protein HemA

Including the following 3 domains:

  1. Glutamyl-tRNA reductase
    Short name=GluTR
    EC=1.2.1.70
  2. Precorrin-2 dehydrogenase
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase
    EC=4.99.1.4
Gene names
Name:hemA
OrganismClostridium josui
Taxonomic identifier1499 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA), the NAD-dependent ring dehydrogenation of precorrin-2 to sirohydrochlorin and finally, the ferrochelation of sirohydrochlorin to yield siroheme Probable. Ref.1

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP-Rule MF_00087

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP-Rule MF_00087

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. HAMAP-Rule MF_00087

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP-Rule MF_00087

Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00087

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.

Sequence similarities

In the N-terminal section; belongs to the glutamyl-tRNA reductase family.

In the C-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Probale multifunctional siroheme biosynthesis protein HemA HAMAP-Rule MF_00087
PRO_0000114012

Regions

Nucleotide binding26 – 272NAD By similarity
Nucleotide binding47 – 482NAD By similarity
Nucleotide binding206 – 2116NADP By similarity
Region26 – 174149Glutamyl-tRNA reductase HAMAP-Rule MF_00087
Region68 – 714Glutamyl-tRNA binding By similarity
Region367 – 507141Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase HAMAP-Rule MF_00087

Sites

Active site691Nucleophile By similarity
Binding site1271Glutamyl-tRNA By similarity
Binding site1321Glutamyl-tRNA By similarity
Binding site1381Glutamyl-tRNA By similarity
Site1171Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59292 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A9769824AA30DC4C

FASTA51558,368
        10         20         30         40         50         60 
MQLGRHNSGS IKKRLEMYIL SIISASLDYK SAAIDIRERF SYTSTRIREI LRRIKAADGV 

        70         80         90        100        110        120 
SGAVLLCTCN RTELYISGDN IENMNPALLL CQLSGEEDHK SLMTLFSIRH DSEAIFHLME 

       130        140        150        160        170        180 
VACGLQSMVL FEDRVITQVK NAAAISREEK TIDSTLETLF RLCITAAKKA KTEIKVKAVP 

       190        200        210        220        230        240 
TSAAERAITE LSKKYCFTDK RILVIGNGEI GRLCCKKLIE LGAEITITLR KYKHGEIIIP 

       250        260        270        280        290        300 
VGCNTIPYDE REEVLPLSDV VISATTSPHF TITYDMIEKL ERKPEIFVDL ALPRDIESSI 

       310        320        330        340        350        360 
SNFTGVELYN LDRFYTDYSV LNQKEVSKIR EIINHFILQF EKWKDYREEA AFTKIPDLHN 

       370        380        390        400        410        420 
DTLYGRFPLF IDLSGKKVLV VGGGEIATRR VKTLLRFGAD IYLVAPHLTS ELQEMLNCKL 

       430        440        450        460        470        480 
INYREGYYES QDIQNMFLVI AATNDRETNH KVYLDAKEKG IQMSIADCRE ECSFYFPAIF 

       490        500        510 
EFDGIVGGLV SQNGDNHSLV KSVAEQIRKI GQATD 

« Hide

References

[1]"Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: FERM P-9684.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28503 Genomic DNA. Translation: BAA05860.1.
PIRI40809.

3D structure databases

ProteinModelPortalQ59292.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00148; UER00222.
UPA00251; UER00316.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
IPR006367. Sirohaem_synthase_N.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01470. cysG_Nterm. 1 hit.
TIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEMA_CLOJO
AccessionPrimary (citable) accession number: Q59292
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways