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Q5NGB9

- GSA_FRATT

UniProt

Q5NGB9 - GSA_FRATT

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene
hemL, FTT_0927
Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
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

BioCyciFTUL177416:GNBP-945-MONOMER.
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:FTT_0927
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001174: Chromosome

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 – 431431Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotationPRO_0000243571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiQ5NGB9. 4 interactions.
STRINGi177416.FTT_0927.

Structurei

3D structure databases

ProteinModelPortaliQ5NGB9.
SMRiQ5NGB9. Positions 1-424.

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.

Q5NGB9-1 [UniParc]FASTAAdd to Basket

« Hide

MENKSNSQIL FAEAQQYIPG GVNSPVRAFK SVGQEFPRFI KFAKGAYLYD    50
VDWNKYIDYI GSWGPMILGH CDDDVLEAIQ CQVKNGLSYG APCKQEVDLA 100
KKIIELMPNI EQVRFVNSGT EATMSAIRLA RAYTCRNKII KFEGCYHGHA 150
DEFLVAAGSG ALSLGQPNSP GVPEDVVKDT LVASFNDMES IQALFEKYKD 200
EIACIIIEPI AGNMNMIFPQ DDFLAKLRAI CDQNSSLLIF DEVMTGFRVA 250
LGGAQSIYNV KPDLTTLGKV IGGGMPVGAF GGRKEIMQKV SPAGPVYQAG 300
TLSGNPIAMT AGIKTLEKIS QPGFFDELGA KAQKLVDGLN EAAKAYDFNF 350
HAKCLGGMFG LFFCSDKIAV NTFVDLGKTN LKMFNQFFAY MLDNGVYLAP 400
SAYEAGFISI AHSDEDIEKT IYLAKKFFQE N 431
Length:431
Mass (Da):47,186
Last modified:February 1, 2005 - v1
Checksum:iB88FE73756171C25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ749949 Genomic DNA. Translation: CAG45560.1.
RefSeqiYP_169923.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45560; CAG45560; FTT_0927.
GeneIDi3192422.
KEGGiftu:FTT_0927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ749949 Genomic DNA. Translation: CAG45560.1 .
RefSeqi YP_169923.1. NC_006570.2.

3D structure databases

ProteinModelPortali Q5NGB9.
SMRi Q5NGB9. Positions 1-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q5NGB9. 4 interactions.
STRINGi 177416.FTT_0927.

Protocols and materials databases

DNASUi 3192422.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG45560 ; CAG45560 ; FTT_0927 .
GeneIDi 3192422.
KEGGi ftu:FTT_0927.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci FTUL177416:GNBP-945-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCHU S4 / Schu 4.

Entry informationi

Entry nameiGSA_FRATT
AccessioniPrimary (citable) accession number: Q5NGB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 76 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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