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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Burkholderia phytofirmans (strain DSM 17436 / PsJN)
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

BioCyciBPHY398527:GJEX-3141-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:Bphyt_3098
OrganismiBurkholderia phytofirmans (strain DSM 17436 / PsJN)
Taxonomic identifieri398527 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001739: Chromosome 1

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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi398527.Bphyt_3098.

Structurei

3D structure databases

ProteinModelPortaliB2T6C2.
SMRiB2T6C2. Positions 3-421.
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.

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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2T6C2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRNETLFER AQRTIPGGVN SPVRAFRSVG GTPRFIERAQ GPYFWDADGQ
60 70 80 90 100
RYIDYIGSWG PMILGHVHPE VLEAVQRVLG NGFSFGAPTE SEVEIAEEIC
110 120 130 140 150
KLVPSIEQVR MVSSGTEATM SALRLARGFT NRSRIVKFEG CYHGHADSLL
160 170 180 190 200
VKAGSGLLTF GNPTSAGVPA DIAKHTTVLE YNNVAELEEA FKAFGNEIAS
210 220 230 240 250
VIVEPVAGNM NLVRATPEFL QALRRLCTEH GSVLIFDEVM CGFRVALGGA
260 270 280 290 300
QEVYGITPDL TCLGKVIGGG MPAAAFGGRR DIMAHLAPLG GVYQAGTLSG
310 320 330 340 350
NPIAVAAGLK TLQLIQAPGF YDTLATRTAR LVQGLANVAR EAKVPFAADS
360 370 380 390 400
LGGMFGLYFT DSIPTSFAEV TKSDVPRFNA FFHKMLDAGV YFAPSAYEAG
410 420
FVSIVHDDAI VDATIDAARG AFASLAA
Length:427
Mass (Da):45,462
Last modified:July 1, 2008 - v1
Checksum:i763F35916CD38B46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001052 Genomic DNA. Translation: ACD17490.1.
RefSeqiWP_012434065.1. NC_010681.1.
YP_001896714.1. NC_010681.1.

Genome annotation databases

EnsemblBacteriaiACD17490; ACD17490; Bphyt_3098.
GeneIDi6283039.
KEGGibpy:Bphyt_3098.
PATRICi19216654. VBIBurPhy117947_7077.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001052 Genomic DNA. Translation: ACD17490.1.
RefSeqiWP_012434065.1. NC_010681.1.
YP_001896714.1. NC_010681.1.

3D structure databases

ProteinModelPortaliB2T6C2.
SMRiB2T6C2. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi398527.Bphyt_3098.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD17490; ACD17490; Bphyt_3098.
GeneIDi6283039.
KEGGibpy:Bphyt_3098.
PATRICi19216654. VBIBurPhy117947_7077.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBPHY398527:GJEX-3141-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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
    , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17436 / PsJN.

Entry informationi

Entry nameiGSA_BURPP
AccessioniPrimary (citable) accession number: B2T6C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: February 4, 2015
This is version 50 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.