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A4SJ79

- GSA_AERS4

UniProt

A4SJ79 - GSA_AERS4

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Aeromonas salmonicida (strain A449)
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

BioCyciASAL382245:GJJN-793-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:ASA_0797
OrganismiAeromonas salmonicida (strain A449)
Taxonomic identifieri382245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
ProteomesiUP000000225: 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000300891Add
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

STRINGi382245.ASA_0797.

Structurei

3D structure databases

ProteinModelPortaliA4SJ79.
SMRiA4SJ79. Positions 2-422.
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.

A4SJ79-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKSDQLFEQ ARQTIPGGVN SPVRAFNGVG GTPRFIDHAD GAYLYDVDGQ
60 70 80 90 100
AYVDYIGSWG PMLLGHNHPA IKAAVIKAVE KGLSYGAPTE IEVLMAEKVR
110 120 130 140 150
QIVPSMEQVR MVNSGTEATM SAIRLARGYT GRDKIVKFEG CYHGHADSLL
160 170 180 190 200
VKAGSGALTL GQPNSPGVPA DFAKHTLTCV FNDLDSVREA FTQYGCDIAC
210 220 230 240 250
IIVEPVAGNM NCIPPVPGFL EGLRTICDEF GALLILDEVM TGFRVSLRGA
260 270 280 290 300
QGYYNIDPDL TTLGKIIGAG MPVGAFGGKK KVMQHIAPTG PVYQAGTLSG
310 320 330 340 350
NPVAMAAGLT MLDLLLEPGL YEQLNAKTAR VAEGLKAAAA KHGIPLAINY
360 370 380 390 400
VGGMFGFFFT DEPEITRYEQ VTRCDMERFK RFYHLMLEEG VYLAPSAYEA
410 420
GFLSLAHGDK EIEHTLAAAE RSFAKLAG
Length:428
Mass (Da):45,936
Last modified:May 15, 2007 - v1
Checksum:i6C989B27AABFF4AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO88951.1.
RefSeqiWP_005313142.1. NC_009348.1.
YP_001140699.1. NC_009348.1.

Genome annotation databases

EnsemblBacteriaiABO88951; ABO88951; ASA_0797.
GeneIDi4996551.
KEGGiasa:ASA_0797.
PATRICi20787930. VBIAerSal2987_0800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO88951.1 .
RefSeqi WP_005313142.1. NC_009348.1.
YP_001140699.1. NC_009348.1.

3D structure databases

ProteinModelPortali A4SJ79.
SMRi A4SJ79. Positions 2-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 382245.ASA_0797.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO88951 ; ABO88951 ; ASA_0797 .
GeneIDi 4996551.
KEGGi asa:ASA_0797.
PATRICi 20787930. VBIAerSal2987_0800.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci ASAL382245:GJJN-793-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. "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
    Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
    BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A449.

Entry informationi

Entry nameiGSA_AERS4
AccessioniPrimary (citable) accession number: A4SJ79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 15, 2007
Last modified: November 26, 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