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Q3B1A1 (GSA_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:Plut_2038
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243595

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B1A1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 509A8BCF8A5C4F6A

FASTA43146,116
        10         20         30         40         50         60 
MPTHTRSAEL FEKAKKFIPG GVNSPVRAFK SVGGNPIFMA KGQGAYMTDV DGNTYLDYVG 

        70         80         90        100        110        120 
SWGPFILGSM HPRITAALEH TLTKIGTSFG TPIEMEIEIA ELLTKIVPSI EMVRMVNSGT 

       130        140        150        160        170        180 
EATMSAVRLA RGCTGRDKII KFEGCYHGHG DSFLIKAGSG ALTLGAPDSP GVTKGTAEDT 

       190        200        210        220        230        240 
LNAKYNDIKS VELLVAENKG NIAAIIIEPV AGNTGVIPAK KEFLQALRDL CDREGIVLIF 

       250        260        270        280        290        300 
DEVMCGFRVA LGGAQELYGI TPDLTTMGKI IGGGLPVGAF GGKRSLMENV APLGGVYQAG 

       310        320        330        340        350        360 
TLSGNPLALT AGIETLKILM EENPYPELDR KGAFLEAGFR DNMQKLGLNF VQNRVGSMAC 

       370        380        390        400        410        420 
LFFTETPVES YDSAITADTE KFGKYFSSML EQGIYLAPSQ FEAMFTSTMH TDADLEKTVK 

       430 
ANYVALQAAT K 

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000096 Genomic DNA. Translation: ABB24880.1.
RefSeqYP_375923.1. NC_007512.1.

3D structure databases

ProteinModelPortalQ3B1A1.
SMRQ3B1A1. Positions 1-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319225.Plut_2038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB24880; ABB24880; Plut_2038.
GeneID3746085.
KEGGplt:Plut_2038.
PATRIC21381736. VBIChlLut1287_2116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycPLUT319225:GHDM-2041-MONOMER.
UniPathwayUPA00251; UER00317.
UPA00668.

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_PELLD
AccessionPrimary (citable) accession number: Q3B1A1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 68 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