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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Helicobacter pylori (strain P12)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processPorphyrin biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciHPYL570508:G1GU0-326-MONOMER
UniPathwayi
UPA00251;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:HPP12_0305
OrganismiHelicobacter pylori (strain P12)
Taxonomic identifieri570508 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000008198 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001218941 – 430Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei265N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB6JKN5
SMRiB6JKN5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000020210
KOiK01845
OMAiWGPLIFG

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00375 HemL_aminotrans_3, 1 hit
InterProiView protein in InterPro
IPR004639 4pyrrol_synth_GluAld_NH2Trfase
IPR005814 Aminotrans_3
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00713 hemL, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit

Sequencei

Sequence statusi: Complete.

B6JKN5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELLHSINDF NEAKQVIAGG VNSPVRAFKS VKGTPPFILK GKGAYLYDVD
60 70 80 90 100
NNHYIDFVQS WGPLIFGHAD EEIEENIINT LKKGTSFGAP TELETTLAKE
110 120 130 140 150
IISCYEGLDK VRLVNSGTEA TMSAIRLARA YSQKDDLIKF EGCYHGHSDS
160 170 180 190 200
LLVKAGSGCA TFGSPSSLGV PNDFSKHTLV ARYNDLNSTE ECFKKGDVGC
210 220 230 240 250
VIIEPIAGNM GLVPAQKEFL LGLKALCEKY QAVLILDEVM SGFRASLSGS
260 270 280 290 300
QEFYGVVPDL VTFGKVIGAG LPLACFGGRA EIMDLLSPIG GVYQAGTLSG
310 320 330 340 350
NPLAVCAGLS ALYKIKRDKT LYTRLNALAV RLTQGLKRSA QNYNIALETL
360 370 380 390 400
NRGSMFGFFF NENAVCDFDD ALKSDTEMFA KFHQKMLFKG VYLACSSFET
410 420 430
GFICEPMTEE MIDLVVAKAD ESFDEIIKGV
Length:430
Mass (Da):46,743
Last modified:December 16, 2008 - v1
Checksum:iD545D7B71F8DAA7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001217 Genomic DNA Translation: ACJ07463.1
RefSeqiWP_000421466.1, NC_011498.1

Genome annotation databases

EnsemblBacteriaiACJ07463; ACJ07463; HPP12_0305
KEGGihpp:HPP12_0305

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001217 Genomic DNA Translation: ACJ07463.1
RefSeqiWP_000421466.1, NC_011498.1

3D structure databases

ProteinModelPortaliB6JKN5
SMRiB6JKN5
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ07463; ACJ07463; HPP12_0305
KEGGihpp:HPP12_0305

Phylogenomic databases

HOGENOMiHOG000020210
KOiK01845
OMAiWGPLIFG

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00317

BioCyciHPYL570508:G1GU0-326-MONOMER

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00375 HemL_aminotrans_3, 1 hit
InterProiView protein in InterPro
IPR004639 4pyrrol_synth_GluAld_NH2Trfase
IPR005814 Aminotrans_3
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00713 hemL, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGSA_HELP2
AccessioniPrimary (citable) accession number: B6JKN5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: October 10, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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