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Q17X40

- GSA_HELAH

UniProt

Q17X40 - GSA_HELAH

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Helicobacter acinonychis (strain Sheeba)
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

BioCyciHACI382638:GJAU-941-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:Hac_1022
OrganismiHelicobacter acinonychis (strain Sheeba)
Taxonomic identifieri382638 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000775: 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000300919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi382638.Hac_1022.

Structurei

3D structure databases

ProteinModelPortaliQ17X40.
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.

Q17X40-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLHSINDF NEAKQVIVGG VNSPVRAFKS VKGTPPFILK GKGAYLYDVD
60 70 80 90 100
NNHYIDFVQS WGPLIFGHAD EEIEENIIKA LKKGTSFGAP TELETTLAKE
110 120 130 140 150
IISCYDGLDK VRLVNSGTEA TMSAIRLARA YSQKDDLIKF EGCYHGHSDS
160 170 180 190 200
LLVKAGSGCT TFGSPSSLGV PSDFSKHTLV ARYNDLNSVQ ECFQKGNVGC
210 220 230 240 250
VIIEPIAGNM GLVPAQKEFL VGLKALCEKY QAVLILDEVM SGFRASLSGS
260 270 280 290 300
QEFYGVVPDL VTFGKVIGAG LPLACFGGRA EIMDLLSPIG GVYQAGTLSG
310 320 330 340 350
NPLAVCAGLS TLYKIKRDKT LYSRLNALAI RLTQGLKKSA KSYNIALQTL
360 370 380 390 400
NRGSMFGFFF NENAVCDFDD ALKSNTEMFA KFHQKMLFKG VYLACSSFET
410 420 430
GFICEPMTEE MIDLVIVKAN ESFDEIIKGV
Length:430
Mass (Da):46,740
Last modified:July 25, 2006 - v1
Checksum:iB8AAAC02BF054A36
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM260522 Genomic DNA. Translation: CAJ99786.1.
RefSeqiWP_011577896.1. NC_008229.1.
YP_664785.1. NC_008229.1.

Genome annotation databases

EnsemblBacteriaiCAJ99786; CAJ99786; Hac_1022.
GeneIDi4177428.
KEGGihac:Hac_1022.
PATRICi20585886. VBIHelAci71660_0957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM260522 Genomic DNA. Translation: CAJ99786.1 .
RefSeqi WP_011577896.1. NC_008229.1.
YP_664785.1. NC_008229.1.

3D structure databases

ProteinModelPortali Q17X40.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 382638.Hac_1022.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ99786 ; CAJ99786 ; Hac_1022 .
GeneIDi 4177428.
KEGGi hac:Hac_1022.
PATRICi 20585886. VBIHelAci71660_0957.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci HACI382638:GJAU-941-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. "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
    Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
    PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sheeba.

Entry informationi

Entry nameiGSA_HELAH
AccessioniPrimary (citable) accession number: Q17X40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 25, 2006
Last modified: October 29, 2014
This is version 60 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