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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule 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

BioCyciHPAR557723:GH24-1765-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:HAPS_1765
OrganismiHaemophilus parasuis serovar 5 (strain SH0165)
Taxonomic identifieri557723 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000006743 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000201022Add
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

STRINGi557723.HAPS_1765.

Structurei

3D structure databases

ProteinModelPortaliB8F7H5.
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.
OMAiCGHAHPE.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B8F7H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSQSLFEK AQRVIPGGVN SPVRAFKGVG GTPVFIDSAK GAYITDSEGK
60 70 80 90 100
RYIDYVGSWG PMVLGHNHPA IIDAVLKAVP NGLSFGAPTA IEIELAELVC
110 120 130 140 150
KLVPSIEMVR MVSSGTEATM SAIRLARGYT KRDKIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGALTL GQPSSPGVPE DFAKHTLTCE YNNLASVKQA FEQYPNDIAC
210 220 230 240 250
LIIEPVAGNM NCIPPKEGFL QGLRELCTQY GAVFIIDEVM TGFRVALGGA
260 270 280 290 300
QSYYGVTPDL TTLGKIIGGG MPVGAFGGKK EIMEFIAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMSAGLA CLTELSKAGN EQLLAEKTKT LAEGFKALAD KHGIPMTVQY
360 370 380 390 400
VGGMFGLFFT EQTKIESYQD VMKCDVKAFN TFFHKMLEKG VYLAPSAFEA
410 420
GFMSLAHSDE DIAYTLEMAD LALAEMK
Length:427
Mass (Da):45,611
Last modified:March 3, 2009 - v1
Checksum:iDF103D89BA787674
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001321 Genomic DNA. Translation: ACL33277.1.
RefSeqiYP_002476225.1. NC_011852.1.

Genome annotation databases

EnsemblBacteriaiACL33277; ACL33277; HAPS_1765.
KEGGihap:HAPS_1765.
PATRICi20195847. VBIHaePar127548_1743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001321 Genomic DNA. Translation: ACL33277.1.
RefSeqiYP_002476225.1. NC_011852.1.

3D structure databases

ProteinModelPortaliB8F7H5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi557723.HAPS_1765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL33277; ACL33277; HAPS_1765.
KEGGihap:HAPS_1765.
PATRICi20195847. VBIHaePar127548_1743.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciHPAR557723:GH24-1765-MONOMER.

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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Haemophilus parasuis SH0165."
    Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., Jin M., Jin Q., Chen H.
    J. Bacteriol. 191:1359-1360(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SH0165.

Entry informationi

Entry nameiGSA_HAEPS
AccessioniPrimary (citable) accession number: B8F7H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 1, 2015
This is version 47 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.