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A9R1E6

- GSA_YERPG

UniProt

A9R1E6 - GSA_YERPG

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - 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

BioCyciYPES349746:GHPB-995-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:YpAngola_A0995
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121934Add
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

STRINGi349746.YpAngola_A0995.

Structurei

3D structure databases

ProteinModelPortaliA9R1E6.
SMRiA9R1E6. 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.
OMAiRAIKPYP.
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.

A9R1E6-1 [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:February 5, 2008 - v1
Checksum:i1BB579AE82D49BA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX88310.1.
RefSeqiYP_001605556.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX88310; ABX88310; YpAngola_A0995.
GeneIDi5799458.
KEGGiypg:YpAngola_A0995.
PATRICi18571038. VBIYerPes97331_1314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX88310.1 .
RefSeqi YP_001605556.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R1E6.
SMRi A9R1E6. Positions 2-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A0995.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX88310 ; ABX88310 ; YpAngola_A0995 .
GeneIDi 5799458.
KEGGi ypg:YpAngola_A0995.
PATRICi 18571038. VBIYerPes97331_1314.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OMAi RAIKPYP.
OrthoDBi EOG6QVRHN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci YPES349746:GHPB-995-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPi MF_00375. HemL_aminotrans_3.
InterProi IPR004639. 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 ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00713. hemL. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiGSA_YERPG
AccessioniPrimary (citable) accession number: A9R1E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 54 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