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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Yersinia pestis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

BioCyciYPES214092:GKDD-3343-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:YPO3389, y0799, YP_0296
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000815: Chromosome, UP000001019: Chromosome, UP000002490: 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120474Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiQ8ZBL9.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ8ZBL9. 1 interaction.
STRINGi214092.YPO3389.

Structurei

Secondary structure

1
426
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Helixi16 – 183Combined sources
Helixi22 – 254Combined sources
Turni26 – 294Combined sources
Beta strandi36 – 416Combined sources
Beta strandi43 – 464Combined sources
Beta strandi51 – 566Combined sources
Helixi57 – 593Combined sources
Helixi69 – 7911Combined sources
Helixi90 – 10213Combined sources
Beta strandi107 – 1148Combined sources
Helixi115 – 13016Combined sources
Beta strandi134 – 1385Combined sources
Helixi170 – 1734Combined sources
Beta strandi176 – 1794Combined sources
Helixi184 – 19310Combined sources
Turni195 – 1973Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi205 – 2073Combined sources
Helixi219 – 23012Combined sources
Beta strandi233 – 2386Combined sources
Turni239 – 2446Combined sources
Helixi250 – 2534Combined sources
Beta strandi259 – 2646Combined sources
Helixi265 – 2684Combined sources
Beta strandi274 – 2785Combined sources
Helixi280 – 2834Combined sources
Turni287 – 2893Combined sources
Beta strandi290 – 2923Combined sources
Helixi302 – 31514Combined sources
Helixi320 – 34122Combined sources
Beta strandi347 – 3515Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi361 – 3633Combined sources
Helixi368 – 3725Combined sources
Helixi376 – 38813Combined sources
Helixi409 – 42315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E77X-ray2.00A1-426[»]
ProteinModelPortaliQ8ZBL9.
SMRiQ8ZBL9. Positions 2-421.
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.

Q8ZBL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSENLYAQ AQQLIPGGVN SPVRAFTGVG GIPLFIERAD GAYLFDVDGK
60 70 80 90 100
AYIDYVGSWG PMILGHNHPA IRQAVIEAVE RGLSFGAPTE MEVKMAQLVT
110 120 130 140 150
DLVPTMDMVR MVNSGTEATM SAIRLARGYT GRDKIIKFEG CYHGHADCLL
160 170 180 190 200
VKAGSGALTL GQPNSPGVPT DFAKHTLTCT YNDLASVRQA FEQYPQEVAC
210 220 230 240 250
IIVEPVAGNM NCIPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA
260 270 280 290 300
QDYYHVIPDL TCLGKIIGGG MPVGAFGGRR EVMNALAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMAAGFA CLTEISQVGV YETLTELTDS LATGLRHAAK EENIPLVVNH
360 370 380 390 400
VGGMFGLFFT NADTVTCYQD VMNCDVERFK RFFHLMLEEG VYLAPSAFEA
410 420
GFMSLAHSNE DIQKTVNAAR RCFAKL
Length:426
Mass (Da):45,794
Last modified:March 1, 2002 - v1
Checksum:i1BB579AE82D49BA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL21978.1.
AE009952 Genomic DNA. Translation: AAM84386.1.
AE017042 Genomic DNA. Translation: AAS60571.1.
PIRiAG0411.
RefSeqiNP_668135.1. NC_004088.1.
NP_991694.1. NC_005810.1.
WP_002209362.1. NZ_KN150724.1.
YP_002348281.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM84386; AAM84386; y0799.
AAS60571; AAS60571; YP_0296.
GeneIDi1145746.
1176206.
2766035.
KEGGiype:YPO3389.
ypk:y0799.
ypm:YP_0296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL21978.1.
AE009952 Genomic DNA. Translation: AAM84386.1.
AE017042 Genomic DNA. Translation: AAS60571.1.
PIRiAG0411.
RefSeqiNP_668135.1. NC_004088.1.
NP_991694.1. NC_005810.1.
WP_002209362.1. NZ_KN150724.1.
YP_002348281.1. NC_003143.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E77X-ray2.00A1-426[»]
ProteinModelPortaliQ8ZBL9.
SMRiQ8ZBL9. Positions 2-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8ZBL9. 1 interaction.
STRINGi214092.YPO3389.

Proteomic databases

PRIDEiQ8ZBL9.

Protocols and materials databases

DNASUi1145746.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM84386; AAM84386; y0799.
AAS60571; AAS60571; YP_0296.
GeneIDi1145746.
1176206.
2766035.
KEGGiype:YPO3389.
ypk:y0799.
ypm:YP_0296.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciYPES214092:GKDD-3343-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CO-92 / Biovar Orientalis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KIM10+ / Biovar Mediaevalis.
  3. "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
    Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R.
    , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
    DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 91001 / Biovar Mediaevalis.

Entry informationi

Entry nameiGSA_YERPE
AccessioniPrimary (citable) accession number: Q8ZBL9
Secondary accession number(s): Q0WBQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 102 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.