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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciNEUR228410:GJNO-1453-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:NE1423
OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Taxonomic identifieri228410 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001416 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi228410.NE1423.

Structurei

3D structure databases

ProteinModelPortaliQ82UQ8.
SMRiQ82UQ8. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ82UQ8.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q82UQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTITNQQLFE RSRQYIPGGV NSPVRAFKSV GGTPVFFQRG QGAYFWDVEG
60 70 80 90 100
KSYIDYVGSW GPLILGHAHP DVVRAVQIAA GHGTSFGAPT AAELEIAELL
110 120 130 140 150
CRLLPSLEMV RLVSSGTEAG MSAIRLARGY TGRNRIIKFE GCYHGHDDAL
160 170 180 190 200
LVKAGSGALT FGHPSSAGVP AETAGHTLVL NYNDVAGVEE TFSKMGTEIA
210 220 230 240 250
AVIVEPVAGN MNLIKATSQF LETLRTLCTK HGSLLILDEV MTGFRVGLEC
260 270 280 290 300
AQGLYGIKPD LTILGKVIGG GLPMAAFGGR RDVMECLAPL GSVYQAGTLS
310 320 330 340 350
GNPVAVAAGL ETLHQIQVPG FFDKLSTMTR KLTEGLTAVA AKHSVAFCAQ
360 370 380 390 400
AVGGMFGLYF RKSPPESFAE VMESDREAFN HFFHAMLKEG VYFAPSAFEA
410 420 430
GFVSAAHSNE EIDKTLAVAD RIFGQGMRRT EKATL
Length:435
Mass (Da):46,402
Last modified:May 31, 2003 - v1
Checksum:iDF24696FAB64C66D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85334.1.
RefSeqiNP_841464.1. NC_004757.1.

Genome annotation databases

EnsemblBacteriaiCAD85334; CAD85334; NE1423.
KEGGineu:NE1423.
PATRICi22714015. VBINitEur56163_1601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85334.1.
RefSeqiNP_841464.1. NC_004757.1.

3D structure databases

ProteinModelPortaliQ82UQ8.
SMRiQ82UQ8. Positions 4-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi228410.NE1423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD85334; CAD85334; NE1423.
KEGGineu:NE1423.
PATRICi22714015. VBINitEur56163_1601.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiQ82UQ8.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciNEUR228410:GJNO-1453-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
    Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
    J. Bacteriol. 185:2759-2773(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19718 / NBRC 14298.

Entry informationi

Entry nameiGSA_NITEU
AccessioniPrimary (citable) accession number: Q82UQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2006
Last sequence update: May 31, 2003
Last modified: March 31, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.