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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Bacillus subtilis (strain 168)
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.

Cofactori

Pathwayi

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

BioCyciBSUB:BSU28120-MONOMER.
BRENDAi5.4.3.8. 658.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Synonyms:hemK
Ordered Locus Names:BSU28120
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU28120. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120393Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiP30949.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU28120.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Helixi19 – 213Combined sources
Beta strandi22 – 243Combined sources
Helixi25 – 284Combined sources
Turni30 – 334Combined sources
Beta strandi39 – 446Combined sources
Beta strandi46 – 494Combined sources
Beta strandi54 – 596Combined sources
Helixi60 – 623Combined sources
Helixi72 – 8413Combined sources
Helixi93 – 10513Combined sources
Beta strandi110 – 1167Combined sources
Helixi118 – 13316Combined sources
Beta strandi137 – 1426Combined sources
Helixi150 – 1523Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi179 – 1835Combined sources
Helixi187 – 19711Combined sources
Helixi198 – 2003Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2143Combined sources
Helixi222 – 23312Combined sources
Beta strandi236 – 2405Combined sources
Turni242 – 2476Combined sources
Helixi252 – 2565Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 2714Combined sources
Beta strandi277 – 2815Combined sources
Helixi283 – 2864Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 2953Combined sources
Helixi305 – 31612Combined sources
Helixi320 – 34324Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi356 – 3649Combined sources
Helixi369 – 3724Combined sources
Helixi377 – 38913Combined sources
Beta strandi396 – 4005Combined sources
Helixi410 – 42920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BS8X-ray2.30A1-430[»]
ProteinModelPortaliP30949.
SMRiP30949. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30949.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiP30949.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiP30949.

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.

P30949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSYEKSKTA FKEAQKLMPG GVNSPVRAFK SVDMDPIFME RGKGSKIFDI
60 70 80 90 100
DGNEYIDYVL SWGPLILGHT NDRVVESLKK VAEYGTSFGA PTEVENELAK
110 120 130 140 150
LVIDRVPSVE IVRMVSSGTE ATMSALRLAR GYTGRNKILK FEGCYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VPEGIAKNTI TVPYNDLESV KLAFQQFGED
210 220 230 240 250
IAGVIVEPVA GNMGVVPPQE GFLQGLRDIT EQYGSLLIFD EVMTGFRVDY
260 270 280 290 300
NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEQIA PSGPIYQAGT
310 320 330 340 350
LSGNPLAMTA GLETLKQLTP ESYKNFIKKG DRLEEGISKT AGAHGIPHTF
360 370 380 390 400
NRAGSMIGFF FTNEPVINYE TAKSSDLKLF ASYYKGMANE GVFLPPSQFE
410 420 430
GLFLSTAHTD EDIENTIQAA EKVFAEISRR
Length:430
Mass (Da):46,449
Last modified:July 1, 1993 - v1
Checksum:iFBC7CF1784C46017
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22515.1.
AL009126 Genomic DNA. Translation: CAB14772.1.
PIRiD42728.
RefSeqiNP_390690.1. NC_000964.3.
WP_004398699.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14772; CAB14772; BSU28120.
GeneIDi937490.
KEGGibsu:BSU28120.
PATRICi18977500. VBIBacSub10457_2939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22515.1.
AL009126 Genomic DNA. Translation: CAB14772.1.
PIRiD42728.
RefSeqiNP_390690.1. NC_000964.3.
WP_004398699.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BS8X-ray2.30A1-430[»]
ProteinModelPortaliP30949.
SMRiP30949. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU28120.

Proteomic databases

PaxDbiP30949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14772; CAB14772; BSU28120.
GeneIDi937490.
KEGGibsu:BSU28120.
PATRICi18977500. VBIBacSub10457_2939.

Organism-specific databases

GenoListiBSU28120. [Micado]

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiP30949.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiP30949.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBSUB:BSU28120-MONOMER.
BRENDAi5.4.3.8. 658.

Miscellaneous databases

EvolutionaryTraceiP30949.

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

« Hide 'large scale' publications
  1. "The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III."
    Hansson M., Rutberg L., Schroeder I., Hederstedt L.
    J. Bacteriol. 173:2590-2599(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiGSA_BACSU
AccessioniPrimary (citable) accession number: P30949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 1, 2015
This is version 121 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.