Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

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

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBANT260799:GJAJ-542-MONOMER.
BANT261594:GJ7F-567-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:BA_0531, GBAA_0531, BAS0499
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000594 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000243536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ81YV0. 4 interactions.
STRINGi198094.BA_0531.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Helixi20 – 223Combined sources
Helixi26 – 283Combined sources
Helixi31 – 333Combined sources
Beta strandi41 – 466Combined sources
Beta strandi48 – 514Combined sources
Beta strandi56 – 594Combined sources
Helixi62 – 643Combined sources
Helixi74 – 8613Combined sources
Helixi95 – 10713Combined sources
Beta strandi112 – 1198Combined sources
Helixi120 – 13516Combined sources
Beta strandi139 – 1435Combined sources
Helixi152 – 1554Combined sources
Beta strandi167 – 1704Combined sources
Helixi175 – 1784Combined sources
Beta strandi181 – 1844Combined sources
Helixi189 – 19911Combined sources
Helixi200 – 2023Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi210 – 2123Combined sources
Helixi224 – 23310Combined sources
Turni234 – 2363Combined sources
Beta strandi238 – 2425Combined sources
Turni244 – 2496Combined sources
Beta strandi250 – 2534Combined sources
Helixi255 – 2595Combined sources
Beta strandi264 – 2696Combined sources
Helixi270 – 2734Combined sources
Beta strandi279 – 2835Combined sources
Helixi285 – 2884Combined sources
Turni292 – 2943Combined sources
Beta strandi295 – 2973Combined sources
Turni302 – 3054Combined sources
Helixi307 – 32014Combined sources
Helixi325 – 34622Combined sources
Beta strandi351 – 3566Combined sources
Beta strandi359 – 3679Combined sources
Helixi372 – 3776Combined sources
Helixi380 – 39213Combined sources
Helixi413 – 43220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L44X-ray2.05A/B1-434[»]
ProteinModelPortaliQ81YV0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81YV0.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiEMFAKFF.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81YV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPIA MERGKGAYFW
60 70 80 90 100
DVDGNKYIDY LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF
110 120 130 140 150
AKMLKEAMPA LDKVRFVNSG TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH
160 170 180 190 200
SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE VITVPFNNVE TLKEALDKWG
210 220 230 240 250
HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI YDEVITAFRF
260 270 280 290 300
MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA
310 320 330 340 350
GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAAKHNID
360 370 380 390 400
ITLNRLKGAL TVYFTTNTIE DYDAAQDTDG EMFGKFFKLM LQEGVNLAPS
410 420 430
KYEAWFLTTE HTKEDIEYTI EAVGRAFAAL ADNK
Length:434
Mass (Da):46,432
Last modified:June 1, 2003 - v1
Checksum:i3C6A06070A078FEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP24552.1.
AE017225 Genomic DNA. Translation: AAT52830.1.
AE017334 Genomic DNA. Translation: AAT29625.1.
RefSeqiNP_843066.1. NC_003997.3.
YP_017150.1. NC_007530.2.
YP_026779.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP24552; AAP24552; BA_0531.
AAT29625; AAT29625; GBAA_0531.
AAT52830; AAT52830; BAS0499.
GeneIDi1087796.
2852947.
KEGGiban:BA_0531.
bar:GBAA_0531.
bat:BAS0499.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP24552.1.
AE017225 Genomic DNA. Translation: AAT52830.1.
AE017334 Genomic DNA. Translation: AAT29625.1.
RefSeqiNP_843066.1. NC_003997.3.
YP_017150.1. NC_007530.2.
YP_026779.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L44X-ray2.05A/B1-434[»]
ProteinModelPortaliQ81YV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81YV0. 4 interactions.
STRINGi198094.BA_0531.

Protocols and materials databases

DNASUi1087796.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP24552; AAP24552; BA_0531.
AAT29625; AAT29625; GBAA_0531.
AAT52830; AAT52830; BAS0499.
GeneIDi1087796.
2852947.
KEGGiban:BA_0531.
bar:GBAA_0531.
bat:BAS0499.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiEMFAKFF.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBANT260799:GJAJ-542-MONOMER.
BANT261594:GJ7F-567-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ81YV0.

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]
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 nameiGSA1_BACAN
AccessioniPrimary (citable) accession number: Q81YV0
Secondary accession number(s): Q6I3Q1, Q6KXG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 98 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.