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Q478V1

- GSA_DECAR

UniProt

Q478V1 - GSA_DECAR

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Dechloromonas aromatica (strain RCB)
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 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

BioCyciDARO159087:GI5B-3980-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:Daro_3902
OrganismiDechloromonas aromatica (strain RCB)
Taxonomic identifieri159087 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
ProteomesiUP000000550: 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243567Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi159087.Daro_3902.

Structurei

3D structure databases

ProteinModelPortaliQ478V1.
SMRiQ478V1. Positions 3-420.
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.
OMAiRAIKPYP.
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.

Q478V1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSRNQQLFE RAQRHIPGGV NSPVRAFRSV GGTPCFFQKG VGAKVQDADG
60 70 80 90 100
KWYTDYVGSW GPMILGHAHP DVIAAVQAAV VDGLSFGAPT EKEVDIADLL
110 120 130 140 150
CELVPSMDMV RLVSSGTEAT MSAIRLARGH TGRDVLIKFE GCYHGHSDGL
160 170 180 190 200
LVKAGSGLLT FGNPSSSGVP AGTAETTMVL TYNDPQELAD AFAKHGDKIA
210 220 230 240 250
AVIVEPVVGN MNLIAPTQAF LNAMRDLCTK NGSVLIFDEV MTGFRVGLKS
260 270 280 290 300
AQGLFGITPD LSTFGKVVGG GMPLGAFGGK REIMEKIAPL GPVYQAGTLS
310 320 330 340 350
GNPIATAAGL ATLKLIQAPG FYEALTAKTK ALCDGLVAAA KKHGVAFSAQ
360 370 380 390 400
NIGGMFGLYF AEQCPGTYDE VLACDKEAFN RFFHAMLDAG HYFAPSAFEA
410 420
GFVSAAHSDA DIAGTIAAAD AYFASLK
Length:427
Mass (Da):44,639
Last modified:September 13, 2005 - v1
Checksum:i241B6995104C5F37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48630.1.
RefSeqiYP_287100.1. NC_007298.1.

Genome annotation databases

EnsemblBacteriaiAAZ48630; AAZ48630; Daro_3902.
GeneIDi3567690.
KEGGidar:Daro_3902.
PATRICi21606498. VBIDecAro89105_3889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48630.1 .
RefSeqi YP_287100.1. NC_007298.1.

3D structure databases

ProteinModelPortali Q478V1.
SMRi Q478V1. Positions 3-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 159087.Daro_3902.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ48630 ; AAZ48630 ; Daro_3902 .
GeneIDi 3567690.
KEGGi dar:Daro_3902.
PATRICi 21606498. VBIDecAro89105_3889.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci DARO159087:GI5B-3980-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. "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
    Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
    BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCB.

Entry informationi

Entry nameiGSA_DECAR
AccessioniPrimary (citable) accession number: Q478V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: November 26, 2014
This is version 70 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