Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5FAH9 (GSA_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:NGO0040
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length426 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
Reference 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000120426

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FAH9 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 6ECA50AF8BC4B55B

FASTA42645,010
        10         20         30         40         50         60 
MNRNEILFDR AKAIIPGGVN SPVRAFGSVG GVPRFIKKAE GAYVWDENGT RYTDYVGSWG 

        70         80         90        100        110        120 
PAIVGHAHPE VVEAVREAAL GGLSFGAPTE GEIAIAEQIA EIMPSVERLR LVSSGTEATM 

       130        140        150        160        170        180 
TAIRLARGFT GRDKIIKFEG CYHGHSDSLL VKAGSGLLTF GNPSSAGVPA DFTKHTLVLE 

       190        200        210        220        230        240 
YNNIAQLEEA FAQSGDEIAC VIVEPFVGNM NLVRPTEAFV KALRGLTEKH GAVLIYDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QSLHGITPDL TTMGKVIGGG MPLAAFGGRK DIMECISPLG GVYQAGTLSG 

       310        320        330        340        350        360 
NPIAVAAGLK TLEIIQREGF YENLTALTQR LANGIAAAKA HGIEFAADSV GGMFGLYFAA 

       370        380        390        400        410        420 
HVPRNYADMA RSNIDAFKRF FHGMLDRGIA FGPSAYEAGF VSAAHTPELI DETVAVAVEV 


FKAMAA 

« Hide

References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW88808.1.
RefSeqYP_207220.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5FAH9.
SMRQ5FAH9. Positions 3-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO0040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW88808; AAW88808; NGO0040.
GeneID3282386.
KEGGngo:NGO0040.
PATRIC20332914. VBINeiGon24812_0042.

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.
ProtClustDBPRK00062.

Enzyme and pathway databases

BioCycNGON242231:GI2G-36-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_NEIG1
AccessionPrimary (citable) accession number: Q5FAH9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 66 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