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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Coxiella burnetii (strain Dugway 5J108-111)
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

BioCyciCBUR434922:GJTP-116-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:CBUD_0113
OrganismiCoxiella burnetii (strain Dugway 5J108-111)
Taxonomic identifieri434922 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000008555: Chromosome

Subcellular locationi

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 – 435435Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000079919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiA9KBA0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi434922.CBUD_0113.

Structurei

3D structure databases

ProteinModelPortaliA9KBA0.
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.
OMAiACLMIEP.
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.

A9KBA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDHSAALFN KAQNYMPGGV NSPVRAFGAV GGVPRFIKKA SGPYLIDVDE
60 70 80 90 100
KKYIDYVGSW GPMILGHAHP AVIQAAQEAV QNGLSFGAPC ENEIKLAALI
110 120 130 140 150
GEFMPSIEKV RMVNSGTEAT MSALRLARGV TGRSKIIKFE GCYHGHADCL
160 170 180 190 200
LVNAGSGALT FGMPSSPGVP LGTVQDTLTA TFNDLDSVAA LFEKYSKDIA
210 220 230 240 250
AIIVEPIAGN MNLIPAAPDF LTGLRELCNQ YGSLLIFDEV ITGFRVAKGG
260 270 280 290 300
AQSLYNIRPD LTALGKIIGG GMPVGAYGGR REIMNQLSPE GPVYQAGTLS
310 320 330 340 350
GNPVAMAAGL ATLKELTAEN FYSNLKEKTE RLVMGILSRA KAAKIPLTAN
360 370 380 390 400
FSCGVFGLIF TSEERVTRYA QAVNGNVEHF RSFFHKMLDN GVYLAPSAFE
410 420 430
SGFISAAHTN KEVDKTLDII ENIFSVSETY LRISV
Length:435
Mass (Da):46,459
Last modified:February 5, 2008 - v1
Checksum:i18A6FFD1A1723CD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000733 Genomic DNA. Translation: ABS76621.1.
RefSeqiYP_001423545.1. NC_009727.1.

Genome annotation databases

EnsemblBacteriaiABS76621; ABS76621; CBUD_0113.
GeneIDi5458054.
KEGGicbd:CBUD_0113.
PATRICi17920072. VBICoxBur32972_0160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000733 Genomic DNA. Translation: ABS76621.1.
RefSeqiYP_001423545.1. NC_009727.1.

3D structure databases

ProteinModelPortaliA9KBA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi434922.CBUD_0113.

Proteomic databases

PRIDEiA9KBA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS76621; ABS76621; CBUD_0113.
GeneIDi5458054.
KEGGicbd:CBUD_0113.
PATRICi17920072. VBICoxBur32972_0160.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiACLMIEP.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciCBUR434922:GJTP-116-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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
    Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
    Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Dugway 5J108-111.

Entry informationi

Entry nameiGSA_COXBN
AccessioniPrimary (citable) accession number: A9KBA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 4, 2015
This is version 55 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

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.