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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Geobacillus thermodenitrificans (strain NG80-2)
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

BioCyciGTHE420246:GIXT-531-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 1UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
Short name:
GSA-AT 1UniRule annotation
Gene namesi
Name:hemL1UniRule annotation
Ordered Locus Names:GTNG_0483
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001578 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000382319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi420246.GTNG_0483.

Structurei

3D structure databases

ProteinModelPortaliA4IKL1.
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.
OMAiFNDIDSY.
OrthoDBiEOG6QVRHN.

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.

A4IKL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQWTKSEQLY EEALRHIVGG VNSPSRSYKA VGGGAPVVME RAQGAYFWDV
60 70 80 90 100
DGNKYIDYLA AYGPIITGHA HPHITAAIQR AAETGVLYGT PTPHEITFAK
110 120 130 140 150
MLKEAIPSLE KVRFVNSGTE AVMTTIRVAR AYTGRSKIVK FAGCYHGHSD
160 170 180 190 200
LVLVAAGSGP STLGTPDSAG VPQSIAHEVI TVPYNDVESF REAMNVWGEH
210 220 230 240 250
VAAVLVEPIV GNFGIVLPKP GFLEAVNDIA HEAGALVIYD EVITAFRFMY
260 270 280 290 300
GGAQNLLGIE PDMTAMGKII GGGLPIGAYG GRQDIMEQVA PLGPAYQAGT
310 320 330 340 350
MAGNPASMLA GIACLEVLKQ EGVYEHLDRL GAMLEEGIMT HARQCGLPVT
360 370 380 390 400
INRLKGALTV FFTEEKVENY EQAQRSDGEL FAKFFKLMLK QGVNLAPSKY
410 420
EAWFITLAHT EDDIAYTIDA VGRAFRQL
Length:428
Mass (Da):46,206
Last modified:May 1, 2007 - v1
Checksum:i5E210EF04C10D286
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO65865.1.
RefSeqiYP_001124610.1. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO65865; ABO65865; GTNG_0483.
KEGGigtn:GTNG_0483.
PATRICi21977187. VBIGeoThe136879_0502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO65865.1.
RefSeqiYP_001124610.1. NC_009328.1.

3D structure databases

ProteinModelPortaliA4IKL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420246.GTNG_0483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO65865; ABO65865; GTNG_0483.
KEGGigtn:GTNG_0483.
PATRICi21977187. VBIGeoThe136879_0502.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiFNDIDSY.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciGTHE420246:GIXT-531-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. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
    Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
    Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NG80-2.

Entry informationi

Entry nameiGSA1_GEOTN
AccessioniPrimary (citable) accession number: A4IKL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 1, 2007
Last modified: April 1, 2015
This is version 66 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

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.