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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Bordetella avium (strain 197N)
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

BioCyciBAVI360910:GCKI-3090-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:BAV3016
OrganismiBordetella avium (strain 197N)
Taxonomic identifieri360910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001977 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_0000243550Add
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

STRINGi360910.BAV3016.

Structurei

3D structure databases

ProteinModelPortaliQ2KUS4.
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.

Q2KUS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRNAELFER ASRSIPGGVN SPVRAFRSVG GTPRFIKRAL GPHIWDADGK
60 70 80 90 100
QYIDYLGSWG PAILGHAHPE VVRAVQDAAT GGLSFGAPTE AEVELAELLI
110 120 130 140 150
QRLPSMEQVR LVSSGTEATM TAIRLARGAT GRNKIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGLLTL GNPSSAGVPP EFVAHTITLD YNNLPAVQTA FAEHGRDIAC
210 220 230 240 250
VIVEPVAGNM NLIKPAAGFL EGLRELCTRH GSVLIFDEVM TGFRVGPQGV
260 270 280 290 300
QGLTGITPDL TTLAKVIGGG MPVGAFGGRA DLMRHIAPLG SVYQAGTLSG
310 320 330 340 350
NPVAVAAGLA TLRLIGQPGF YEDLSARTQR LALGLTERAH AAGVTFSADA
360 370 380 390 400
IGGMFGLYFR DKVPTSFAEV QTSNTEAFKR FFHAMLDRGV HFAPSAFEAG
410 420
FVSAAHDDAT LQATLDHAEA AFALLKA
Length:427
Mass (Da):44,954
Last modified:March 7, 2006 - v1
Checksum:i498576BB1E23DB3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ50626.1.
RefSeqiYP_787511.1. NC_010645.1.

Genome annotation databases

EnsemblBacteriaiCAJ50626; CAJ50626; BAV3016.
KEGGibav:BAV3016.
PATRICi21132343. VBIBorAvi43433_3050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ50626.1.
RefSeqiYP_787511.1. NC_010645.1.

3D structure databases

ProteinModelPortaliQ2KUS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi360910.BAV3016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ50626; CAJ50626; BAV3016.
KEGGibav:BAV3016.
PATRICi21132343. VBIBorAvi43433_3050.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBAVI360910:GCKI-3090-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. "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
    Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
    J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 197N.

Entry informationi

Entry nameiGSA_BORA1
AccessioniPrimary (citable) accession number: Q2KUS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: April 1, 2015
This is version 69 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.