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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
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

BioCyciASUC339671:GHDX-1835-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:Asuc_1761
OrganismiActinobacillus succinogenes (strain ATCC 55618 / 130Z)
Taxonomic identifieri339671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
ProteomesiUP000001114: 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000072150Add
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

STRINGi339671.Asuc_1761.

Structurei

3D structure databases

ProteinModelPortaliA6VQ66.
SMRiA6VQ66. Positions 3-422.
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.

A6VQ66-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNSTALFQR ARQVIPGGVN SPVRAFKGVG GTPVFIQKAA GAYITDTDGK
60 70 80 90 100
QYIDYVGSWG PMVLGHNHPA IIDAVLKAVP NGLSFGAPTE GEITLAELVC
110 120 130 140 150
RLIPSIELVR MVSSGTEATM SAIRLARGYT KRDKIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGALTL GQPSSPGVPE DFAKHTLTCT YNDLNSVKCA FERYPQDIAC
210 220 230 240 250
LIIEPVAGNM NCVPPKPGFL QGVRELCDQY GALLIIDEVM TGFRVALGGA
260 270 280 290 300
QAYYGVTPDL TALGKIIGGG MPVGAFGGKR EIMEYIAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMAAGLA CLTELSKPGN EQQLAEKTQQ LAEGLKTLAK KHGVPFIAQY
360 370 380 390 400
VGGMFGLFFT DVPEVTNFQD VMKCDVAKFN RFFHLMLEQG VYLAPSAFEA
410 420
GFMSLAHSDA DIEQTLKAAD NAFAVLA
Length:427
Mass (Da):45,369
Last modified:August 21, 2007 - v1
Checksum:iC303864EE63BB0A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000746 Genomic DNA. Translation: ABR75113.1.
RefSeqiWP_012073490.1. NC_009655.1.
YP_001345048.1. NC_009655.1.

Genome annotation databases

EnsemblBacteriaiABR75113; ABR75113; Asuc_1761.
GeneIDi5348465.
KEGGiasu:Asuc_1761.
PATRICi20761936. VBIActSuc117883_1839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000746 Genomic DNA. Translation: ABR75113.1.
RefSeqiWP_012073490.1. NC_009655.1.
YP_001345048.1. NC_009655.1.

3D structure databases

ProteinModelPortaliA6VQ66.
SMRiA6VQ66. Positions 3-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339671.Asuc_1761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR75113; ABR75113; Asuc_1761.
GeneIDi5348465.
KEGGiasu:Asuc_1761.
PATRICi20761936. VBIActSuc117883_1839.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciASUC339671:GHDX-1835-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. "A genomic perspective on the potential of Actinobacillus succinogenes for industrial succinate production."
    McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., Burkhart K.B., Harkins V., Vieille C.
    BMC Genomics 11:680-680(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 55618 / 130Z.

Entry informationi

Entry nameiGSA_ACTSZ
AccessioniPrimary (citable) accession number: A6VQ66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: February 4, 2015
This is version 52 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.