SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A0PLS0

- GSA_MYCUA

UniProt

A0PLS0 - GSA_MYCUA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene
hemL, MUL_0623
Organism
Mycobacterium ulcerans (strain Agy99)
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 phosphate By similarity.UniRule 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

UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Ordered Locus Names:MUL_0623
OrganismiMycobacterium ulcerans (strain Agy99)
Taxonomic identifieri362242 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000765: Chromosome

Organism-specific databases

GenoListiMUL_0623.

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 443443Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotationPRO_0000300927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi362242.MUL_0623.

Structurei

3D structure databases

ProteinModelPortaliA0PLS0.
SMRiA0PLS0. Positions 12-429.

Family & Domainsi

Sequence similaritiesi

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.

A0PLS0-1 [UniParc]FASTAAdd to Basket

« Hide

MGSTDQAVTS VRRSAQLFTD ACAVIPGGVN SPVRAFTAVG GTPRFITEAH    50
GCWLTDADGN RYADLVCSWG PMILGHAHPA VVEAVSRAAA NGLSFGAPTP 100
TETELAAEMI GRVAPVERLR LVNSGTEATM SAVRLARGFT GRSKIIKFSG 150
CYHGHVDALL ADAGSGVATL GLPSSPGVTG AAAADTIVLP YNDLEAVRQT 200
FAQHGEQIAA VITEASPGNM GVVPPGRGYN AALRAVTAEH GALLIVDEVM 250
TGFRVSRSGW YGIDPVDADL FTFGKVMSGG LPAAAFGGRA EVMERLAPLG 300
PVYQAGTLSG NPVAMAAGLA TLRTADDGVY AALDANADRL ARLLAGALTD 350
AGVAHQIPRA GNMLSVFFSE TPVTDFAAAR NSQTWRFAPF FHALLDAGVY 400
PPCSAFEAWF VSAALDDTAF ERIADALPTA ARAAANATPE SRP 443
Length:443
Mass (Da):45,741
Last modified:January 9, 2007 - v1
Checksum:i23C1090042BB89E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL03289.1.
RefSeqiWP_011738914.1. NC_008611.1.
YP_904760.1. NC_008611.1.

Genome annotation databases

EnsemblBacteriaiABL03289; ABL03289; MUL_0623.
GeneIDi4551620.
KEGGimul:MUL_0623.
PATRICi18167860. VBIMycUlc37413_0798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000325 Genomic DNA. Translation: ABL03289.1 .
RefSeqi WP_011738914.1. NC_008611.1.
YP_904760.1. NC_008611.1.

3D structure databases

ProteinModelPortali A0PLS0.
SMRi A0PLS0. Positions 12-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362242.MUL_0623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL03289 ; ABL03289 ; MUL_0623 .
GeneIDi 4551620.
KEGGi mul:MUL_0623.
PATRICi 18167860. VBIMycUlc37413_0798.

Organism-specific databases

GenoListi MUL_0623.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .

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. "Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
    Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.
    , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
    Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Agy99.

Entry informationi

Entry nameiGSA_MYCUA
AccessioniPrimary (citable) accession number: A0PLS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 56 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

Similar proteinsi