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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

BioCyciBANT260799:GJAJ-4413-MONOMER.
BANT261594:GJ7F-4561-MONOMER.
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:BA_4693, GBAA_4693, BAS4358
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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_0000243537Add
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

IntActiQ81LD0. 22 interactions.
STRINGi198094.BA_4693.

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Turni15 – 173Combined sources
Helixi19 – 213Combined sources
Beta strandi22 – 243Combined sources
Helixi25 – 284Combined sources
Helixi30 – 323Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 494Combined sources
Beta strandi54 – 585Combined sources
Helixi60 – 623Combined sources
Helixi72 – 8413Combined sources
Helixi93 – 10513Combined sources
Beta strandi110 – 1178Combined sources
Helixi118 – 13316Combined sources
Beta strandi137 – 1426Combined sources
Helixi150 – 1523Combined sources
Helixi173 – 1764Combined sources
Beta strandi179 – 1835Combined sources
Helixi187 – 19711Combined sources
Helixi198 – 2003Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi208 – 2103Combined sources
Helixi222 – 23312Combined sources
Beta strandi236 – 2405Combined sources
Turni242 – 2476Combined sources
Helixi252 – 2576Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 2714Combined sources
Beta strandi277 – 2815Combined sources
Helixi283 – 2864Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 2953Combined sources
Turni300 – 3034Combined sources
Helixi305 – 31612Combined sources
Helixi320 – 34324Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi356 – 3649Combined sources
Helixi369 – 3724Combined sources
Helixi377 – 38913Combined sources
Helixi410 – 42516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K28X-ray1.95A/B/C/D1-429[»]
ProteinModelPortaliQ81LD0.
SMRiQ81LD0. Positions 4-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81LD0.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
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.

Q81LD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI
60 70 80 90 100
DGNEYIDYVL SWGPLIHGHA NDRVVEALKA VAERGTSFGA 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 AAKSSNLQFF AAYYREMVEQ GVFLPPSQFE
410 420
GLFLSTVHSD ADIEATIAAA EIAMSKLKA
Length:429
Mass (Da):46,060
Last modified:June 1, 2003 - v1
Checksum:i9E56295469536AD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28392.1.
AE017225 Genomic DNA. Translation: AAT56656.1.
AE017334 Genomic DNA. Translation: AAT33816.1.
RefSeqiNP_846906.1. NC_003997.3.
WP_001224513.1. NZ_KN050651.1.
YP_021341.1. NC_007530.2.
YP_030605.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP28392; AAP28392; BA_4693.
AAT33816; AAT33816; GBAA_4693.
AAT56656; AAT56656; BAS4358.
GeneIDi1083709.
2819770.
2850472.
KEGGiban:BA_4693.
bar:GBAA_4693.
bat:BAS4358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28392.1.
AE017225 Genomic DNA. Translation: AAT56656.1.
AE017334 Genomic DNA. Translation: AAT33816.1.
RefSeqiNP_846906.1. NC_003997.3.
WP_001224513.1. NZ_KN050651.1.
YP_021341.1. NC_007530.2.
YP_030605.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K28X-ray1.95A/B/C/D1-429[»]
ProteinModelPortaliQ81LD0.
SMRiQ81LD0. Positions 4-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81LD0. 22 interactions.
STRINGi198094.BA_4693.

Protocols and materials databases

DNASUi1083709.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP28392; AAP28392; BA_4693.
AAT33816; AAT33816; GBAA_4693.
AAT56656; AAT56656; BAS4358.
GeneIDi1083709.
2819770.
2850472.
KEGGiban:BA_4693.
bar:GBAA_4693.
bat:BAS4358.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBANT260799:GJAJ-4413-MONOMER.
BANT261594:GJ7F-4561-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ81LD0.

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]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.

Entry informationi

Entry nameiGSA2_BACAN
AccessioniPrimary (citable) accession number: Q81LD0
Secondary accession number(s): Q6HST3, Q6KM26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: March 4, 2015
This is version 95 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.