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A9KBA0

- GSA_COXBN

UniProt

A9KBA0 - GSA_COXBN

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Coxiella burnetii (strain Dugway 5J108-111)
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

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-HAMAP
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.
OMAiHGHANAF.
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:
EMBL
GenBank
DDBJ
Links Updated
CP000733 Genomic DNA. Translation: ABS76621.1.
RefSeqiWP_011996416.1. NC_009727.1.
YP_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:
EMBL
GenBank
DDBJ
Links Updated
CP000733 Genomic DNA. Translation: ABS76621.1 .
RefSeqi WP_011996416.1. NC_009727.1.
YP_001423545.1. NC_009727.1.

3D structure databases

ProteinModelPortali A9KBA0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 434922.CBUD_0113.

Proteomic databases

PRIDEi A9KBA0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS76621 ; ABS76621 ; CBUD_0113 .
GeneIDi 5458054.
KEGGi cbd:CBUD_0113.
PATRICi 17920072. VBICoxBur32972_0160.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci CBUR434922:GJTP-116-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. "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: October 29, 2014
This is version 52 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