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Q59292

- HEMA_CLOJO

UniProt

Q59292 - HEMA_CLOJO

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Protein
Probable multifunctional siroheme biosynthesis protein HemA
Gene
hemA
Organism
Clostridium josui
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

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 Inferred.1 Publication

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation
Precorrin-2 + NAD+ = sirohydrochlorin + NADH.UniRule annotation
Siroheme + 2 H+ = sirohydrochlorin + Fe2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Nucleophile By similarity
Sitei117 – 1171Important for activity By similarity
Binding sitei127 – 1271Glutamyl-tRNA By similarity
Binding sitei132 – 1321Glutamyl-tRNA By similarity
Binding sitei138 – 1381Glutamyl-tRNA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272NAD By similarity
Nucleotide bindingi47 – 482NAD By similarity
Nucleotide bindingi206 – 2116NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  3. precorrin-2 dehydrogenase activity Source: UniProtKB-EC
  4. sirohydrochlorin ferrochelatase activity Source: UniProtKB-EC

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-UniPathway
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  3. siroheme biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00148; UER00222.
UPA00251; UER00316.
UPA00262; UER00222.
UPA00262; UER00376.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable multifunctional siroheme biosynthesis protein HemA
Including the following 3 domains:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Precorrin-2 dehydrogenase (EC:1.3.1.76)
Sirohydrochlorin ferrochelatase (EC:4.99.1.4)
Gene namesi
Name:hemA
OrganismiClostridium josui
Taxonomic identifieri1499 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Probable multifunctional siroheme biosynthesis protein HemA
PRO_0000114012Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ59292.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 174149Glutamyl-tRNA reductaseUniRule annotation
Add
BLAST
Regioni68 – 714Glutamyl-tRNA binding By similarity
Regioni367 – 507141Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotation
Add
BLAST

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 By similarity.UniRule annotation

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
IPR006367. Sirohaem_synthase_N.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01470. cysG_Nterm. 1 hit.
TIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59292-1 [UniParc]FASTAAdd to Basket

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MQLGRHNSGS IKKRLEMYIL SIISASLDYK SAAIDIRERF SYTSTRIREI    50
LRRIKAADGV SGAVLLCTCN RTELYISGDN IENMNPALLL CQLSGEEDHK 100
SLMTLFSIRH DSEAIFHLME VACGLQSMVL FEDRVITQVK NAAAISREEK 150
TIDSTLETLF RLCITAAKKA KTEIKVKAVP TSAAERAITE LSKKYCFTDK 200
RILVIGNGEI GRLCCKKLIE LGAEITITLR KYKHGEIIIP VGCNTIPYDE 250
REEVLPLSDV VISATTSPHF TITYDMIEKL ERKPEIFVDL ALPRDIESSI 300
SNFTGVELYN LDRFYTDYSV LNQKEVSKIR EIINHFILQF EKWKDYREEA 350
AFTKIPDLHN DTLYGRFPLF IDLSGKKVLV VGGGEIATRR VKTLLRFGAD 400
IYLVAPHLTS ELQEMLNCKL INYREGYYES QDIQNMFLVI AATNDRETNH 450
KVYLDAKEKG IQMSIADCRE ECSFYFPAIF EFDGIVGGLV SQNGDNHSLV 500
KSVAEQIRKI GQATD 515
Length:515
Mass (Da):58,368
Last modified:November 1, 1997 - v1
Checksum:iA9769824AA30DC4C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28503 Genomic DNA. Translation: BAA05860.1.
PIRiI40809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28503 Genomic DNA. Translation: BAA05860.1 .
PIRi I40809.

3D structure databases

ProteinModelPortali Q59292.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00222 .
UPA00251 ; UER00316 .
UPA00262 ; UER00222 .
UPA00262 ; UER00376 .

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
IPR006367. Sirohaem_synthase_N.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01470. cysG_Nterm. 1 hit.
TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHEMA_CLOJO
AccessioniPrimary (citable) accession number: Q59292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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