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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-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

BioCyciTROS309801:GI0S-1111-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:trd_1123
OrganismiThermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
Taxonomic identifieri309801 [NCBI]
Taxonomic lineageiBacteriaChloroflexiThermomicrobialesThermomicrobiaceaeThermomicrobium
ProteomesiUP000000447 Componenti: Chromosome

Subcellular locationi

  1. 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000201036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi309801.trd_1123.

Structurei

3D structure databases

ProteinModelPortaliB9L0Q2.
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.

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.

B9L0Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMMENSGSLW DAARQFFPGG VNSPVRAFRA VGEEPVVAVR GEGAYLIDAD
60 70 80 90 100
GRRFLDYICS WGALLAGHAH PHVVDRLSEA IQRGTSFGLL SPYEVELARA
110 120 130 140 150
IVASVPAIEL VRFVNSGTEA TMSAIRLARA VTGRNLVVKF AGCYHGHVDG
160 170 180 190 200
LLVAAGSGVL TFGLPGTPGV TEGTARDTLV LPYNDQEAVE DAFAQHGERI
210 220 230 240 250
AAVIVEPVAG NMGVVPPAAG FLSRLRELTR QAGALLIFDE VITGFRLGLG
260 270 280 290 300
GAQERFGILP DLTCLGKVIG GGLPVGAYGG RRDLMEQVAP NGPVYQAGTL
310 320 330 340 350
AGNPLSMVAG LATLELAREP GVYGRLETLA AWLQRGLEET IQESGLPAHV
360 370 380 390 400
QRVGSMLTLF FSQQPVTDAQ TAERCDTARF AAFHRAMRAQ GILLPPSQFE
410 420 430
AWFVSLAHRE EDIDRTIEAA RKALAEVARG
Length:430
Mass (Da):45,749
Last modified:March 24, 2009 - v1
Checksum:iD567EB4C01C5E732
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05709.1.
RefSeqiWP_015922076.1. NC_011959.1.
YP_002522332.1. NC_011959.1.

Genome annotation databases

EnsemblBacteriaiACM05709; ACM05709; trd_1123.
KEGGitro:trd_1123.
PATRICi23913418. VBITheRos91376_1059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05709.1.
RefSeqiWP_015922076.1. NC_011959.1.
YP_002522332.1. NC_011959.1.

3D structure databases

ProteinModelPortaliB9L0Q2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309801.trd_1123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM05709; ACM05709; trd_1123.
KEGGitro:trd_1123.
PATRICi23913418. VBITheRos91376_1059.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciTROS309801:GI0S-1111-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 aerobic CO-oxidizing thermophile Thermomicrobium roseum."
    Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L., Eisen J.A.
    PLoS ONE 4:E4207-E4207(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27502 / DSM 5159 / P-2.

Entry informationi

Entry nameiGSA_THERP
AccessioniPrimary (citable) accession number: B9L0Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: April 29, 2015
This is version 48 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.