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Q65M82

- GSA1_BACLD

UniProt

Q65M82 - GSA1_BACLD

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
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

BioCyciBLIC279010:GJ2P-891-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 1UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
Short name:
GSA-AT 1UniRule annotation
Gene namesi
Name:hemL1UniRule annotation
Ordered Locus Names:BLi00898, BL03060
OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)
Taxonomic identifieri279010 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000000606: Chromosome, UP000000608: 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000243546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279010.BL03060.

Structurei

3D structure databases

ProteinModelPortaliQ65M82.
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.
OMAiETRANGM.
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.

Q65M82-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQHTQSEKLH EEALQHIVGG VNSPSRSYKA VGGGSPVAME RGSGAYFWDV
60 70 80 90 100
DGNKYIDYLA AYGPIITGHA HPHITKAIQT AAENGVLYGT PTKHEVTFAK
110 120 130 140 150
MLKEAIPALD KVRFVNSGTE AVMTTIRVAR AYTGRTKIIK FAGCYHGHSD
160 170 180 190 200
LVLVAAGSGP STLGTPDSAG VPKSIANEVI TVPFNDIDSY KEALDKWGND
210 220 230 240 250
IAAVLVEPIV GNFGIVEPKS GFLEQVNELT HNAGALVIYD EVITAFRFMY
260 270 280 290 300
GGAQDLLGVK PDLTALGKII GGGLPIGAYG GRKEIMEQVA PLGPAYQAGT
310 320 330 340 350
MAGNPASILS GIACLEVLKE KGTYEKLDRL GAMLEEGILA HAETHGIDIT
360 370 380 390 400
VNRLKGALTV YFTNEKVENY EQAENTDGDM FAAFFKLMLE RGINLAPSKY
410 420 430
EAWFITTAHT EEDIKDTLKA VDDSFKQLKQ RM
Length:432
Mass (Da):46,537
Last modified:October 25, 2004 - v1
Checksum:i591A571D03DE60D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU39832.1.
CP000002 Genomic DNA. Translation: AAU22484.1.
RefSeqiYP_006712302.1. NC_006322.1.
YP_078122.1. NC_006270.3.

Genome annotation databases

EnsemblBacteriaiAAU22484; AAU22484; BL03060.
AAU39832; AAU39832; BLi00898.
GeneIDi3029738.
3098858.
KEGGibld:BLi00898.
bli:BL03060.
PATRICi18947339. VBIBacLic203714_0894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU39832.1 .
CP000002 Genomic DNA. Translation: AAU22484.1 .
RefSeqi YP_006712302.1. NC_006322.1.
YP_078122.1. NC_006270.3.

3D structure databases

ProteinModelPortali Q65M82.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279010.BL03060.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU22484 ; AAU22484 ; BL03060 .
AAU39832 ; AAU39832 ; BLi00898 .
GeneIDi 3029738.
3098858.
KEGGi bld:BLi00898.
bli:BL03060.
PATRICi 18947339. VBIBacLic203714_0894.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci BLIC279010:GJ2P-891-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 complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
    Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.

Entry informationi

Entry nameiGSA1_BACLD
AccessioniPrimary (citable) accession number: Q65M82
Secondary accession number(s): Q62XM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2004
Last modified: November 26, 2014
This is version 82 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