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Q4L706

- GSA2_STAHJ

UniProt

Q4L706 - GSA2_STAHJ

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Staphylococcus haemolyticus (strain JCSC1435)
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.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

BioCyciSHAE279808:GJX7-1314-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 2UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 2UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2UniRule annotation
Short name:
GSA-AT 2UniRule annotation
Gene namesi
Name:hemL2UniRule annotation
Ordered Locus Names:SH1260
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000243623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH1260.

Structurei

3D structure databases

ProteinModelPortaliQ4L706.
SMRiQ4L706. Positions 1-426.
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.

Q4L706 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGYEKSIEAM KIAENLMPGG VNSPVRAFKS VDTPAIFMDH AKGSRIYDID
60 70 80 90 100
GNEYIDYVLS WGPLILGHKN EQVIKKLHEA VNRGTSFGAS TLEENKLAEL
110 120 130 140 150
VIERVPSIEK VRMVSSGTEA TLAALRLARG YTGRNKIIKF EGCYHGHSDS
160 170 180 190 200
LLIKAGSGVA TLGLPDSPGV PEGTAKNTIT VPYNDLEAIK IAFENYGDDI
210 220 230 240 250
AGIIVEPVAG NMGVVPPKDG FLQGLREITN DYGALLIFDE VMTGFRVGYN
260 270 280 290 300
CAQGYFGVTP DLTCLGKVIG GGLPVGAFGG RKEIMDKVAP VGNIYQAGTL
310 320 330 340 350
SGNPLAMTSG YETLSQLTPE SYEYFQELGD ILEEGLKKVF SKHNVPITIN
360 370 380 390 400
RAGSMIGYFL NEGPVTNFEE ANKSNLELFS QMYREMAKEG VFLPPSQFEG
410 420
TFLSTAHSKE DIEKTIQAFD TALSRIV
Length:427
Mass (Da):46,278
Last modified:August 2, 2005 - v1
Checksum:i0ECA8BDD77735C1C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE04569.1.
RefSeqiWP_011275558.1. NC_007168.1.
YP_253175.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE04569; BAE04569; SH1260.
GeneIDi3482185.
KEGGisha:SH1260.
PATRICi19618635. VBIStaHae67511_1241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE04569.1 .
RefSeqi WP_011275558.1. NC_007168.1.
YP_253175.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L706.
SMRi Q4L706. Positions 1-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH1260.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE04569 ; BAE04569 ; SH1260 .
GeneIDi 3482185.
KEGGi sha:SH1260.
PATRICi 19618635. VBIStaHae67511_1241.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci SHAE279808:GJX7-1314-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiGSA2_STAHJ
AccessioniPrimary (citable) accession number: Q4L706
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: August 2, 2005
Last modified: October 29, 2014
This is version 74 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