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Q72ZW5

- GSA2_BACC1

UniProt

Q72ZW5 - GSA2_BACC1

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Bacillus cereus (strain ATCC 10987)
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

UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 2UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 2UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2UniRule annotation
Short name:
GSA-AT 2UniRule annotation
Gene namesi
Name:hemL2UniRule annotation
Ordered Locus Names:BCE_4552
OrganismiBacillus cereus (strain ATCC 10987)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527: 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000243539Add
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

STRINGi222523.BCE_4552.

Structurei

3D structure databases

ProteinModelPortaliQ72ZW5.
SMRiQ72ZW5. Positions 1-427.
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.

Q72ZW5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI
60 70 80 90 100
DGNEYIDYVL SWGPLIHGHA NNRVVEALKA VAEKGTSFGA PTEIENKLAK
110 120 130 140 150
LVIERVPSIE IVRMVNSGTE ATMSALRLAR GYTGRNKILK FIGCYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI TVAYNDLESV KYAFEQFGDD
210 220 230 240 250
IACVIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD EVMTGFRVAY
260 270 280 290 300
NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQVA PSGPIYQAGT
310 320 330 340 350
LSGNPLAMAA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHGIPHHI
360 370 380 390 400
NRAGSMIGIF FTDEPVINYD AAKSSNLEFF AAYYREMVEQ GVFLPPSQFE
410 420
GLFLSTAHSD ADIEATIAAA EIAMSKLKA
Length:429
Mass (Da):45,976
Last modified:July 5, 2004 - v1
Checksum:iA95459B3BF7CF14C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS43453.1.
RefSeqiNP_980845.1. NC_003909.8.
WP_000712955.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS43453; AAS43453; BCE_4552.
GeneIDi2750571.
KEGGibca:BCE_4552.
PATRICi18857736. VBIBacCer118379_4365.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS43453.1 .
RefSeqi NP_980845.1. NC_003909.8.
WP_000712955.1. NC_003909.8.

3D structure databases

ProteinModelPortali Q72ZW5.
SMRi Q72ZW5. Positions 1-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 222523.BCE_4552.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS43453 ; AAS43453 ; BCE_4552 .
GeneIDi 2750571.
KEGGi bca:BCE_4552.
PATRICi 18857736. VBIBacCer118379_4365.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .

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 sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987.

Entry informationi

Entry nameiGSA2_BACC1
AccessioniPrimary (citable) accession number: Q72ZW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3