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Q3A7W5 (GSA_PELCD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:Pcar_0266
OrganismPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]
Taxonomic identifier338963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243594

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3A7W5 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 94CC56366A4D7AA2

FASTA42745,299
        10         20         30         40         50         60 
MSYSRSHQFF ERARKVIPGG VNSPVRAFKA VGRQPLFIER AEGCTLVDAD GNRYIDYVGS 

        70         80         90        100        110        120 
WGPMIVGHSH PKVVEAICDA AARGTSFGAP TALEIELAEQ VCAAFPNMES VRMVSSGTEA 

       130        140        150        160        170        180 
TMSAIRLARG VTGRDKILKF EGCYHGHADS LLVDAGSGVA TFGIPASPGV PADFARHTLT 

       190        200        210        220        230        240 
APYNDLGRVR ALVEEHKADL AAIILEPIAG NMGCVPPQPG FLEGLRALCD QHEILLIIDE 

       250        260        270        280        290        300 
VMTGFRVSYG GAQQLYGVRG DLVCLGKVIG GGLPVGAFGG RQDIMRHLAP DGGVYQAGTL 

       310        320        330        340        350        360 
SGNPLAMSAG IATLKLIREE GVYEQLEQRS AYLAEGLRQA AAAAGVPACL QRVGSMFCNY 

       370        380        390        400        410        420 
FQTGPVTSFA DAKASDTEAF ARYFGQMLDN GVHLAPSQFE AGFVSLAHTV EDIDRTVEAA 


HRSLKAI 

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References

[1]"Complete sequence of Pelobacter carbinolicus DSM 2380."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000142 Genomic DNA. Translation: ABA87527.1.
RefSeqYP_006715928.1. NC_007498.2.

3D structure databases

ProteinModelPortalQ3A7W5.
SMRQ3A7W5. Positions 1-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338963.Pcar_0266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA87527; ABA87527; Pcar_0266.
GeneID3722797.
KEGGpca:Pcar_0266.
PATRIC22886416. VBIPelCar86875_0289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAHGHANAF.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPCAR338963:GKDU-295-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 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]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_PELCD
AccessionPrimary (citable) accession number: Q3A7W5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways