SubmitCancel

Skip Header

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

P30949

- GSA_BACSU

UniProt

P30949 - GSA_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamate-1-semialdehyde 2,1-aminomutase
Gene
hemL, hemK, BSU28120
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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 phosphate By similarity.UniRule 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

BioCyciBSUB:BSU28120-MONOMER.
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: Chromosome

Organism-specific databases

GenoListiBSU28120. [Micado]

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation
PRO_0000120393Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiP30949.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi224308.BSU28120.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BS8X-ray2.30A1-430[»]
ProteinModelPortaliP30949.
SMRiP30949. Positions 1-430.

Miscellaneous databases

EvolutionaryTraceiP30949.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiRAIKPYP.
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]
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.

P30949-1 [UniParc]FASTAAdd to Basket

« Hide

MRSYEKSKTA FKEAQKLMPG GVNSPVRAFK SVDMDPIFME RGKGSKIFDI    50
DGNEYIDYVL SWGPLILGHT NDRVVESLKK VAEYGTSFGA PTEVENELAK 100
LVIDRVPSVE IVRMVSSGTE ATMSALRLAR GYTGRNKILK FEGCYHGHGD 150
SLLIKAGSGV ATLGLPDSPG VPEGIAKNTI TVPYNDLESV KLAFQQFGED 200
IAGVIVEPVA GNMGVVPPQE GFLQGLRDIT EQYGSLLIFD EVMTGFRVDY 250
NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEQIA PSGPIYQAGT 300
LSGNPLAMTA GLETLKQLTP ESYKNFIKKG DRLEEGISKT AGAHGIPHTF 350
NRAGSMIGFF FTNEPVINYE TAKSSDLKLF ASYYKGMANE GVFLPPSQFE 400
GLFLSTAHTD EDIENTIQAA EKVFAEISRR 430
Length:430
Mass (Da):46,449
Last modified:July 1, 1993 - v1
Checksum:iFBC7CF1784C46017
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57676 Genomic DNA. Translation: AAA22515.1 .
AL009126 Genomic DNA. Translation: CAB14772.1 .
PIRi D42728.
RefSeqi NP_390690.1. NC_000964.3.
WP_004398699.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BS8 X-ray 2.30 A 1-430 [» ]
ProteinModelPortali P30949.
SMRi P30949. Positions 1-430.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU28120.

Proteomic databases

PaxDbi P30949.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14772 ; CAB14772 ; BSU28120 .
GeneIDi 937490.
KEGGi bsu:BSU28120.
PATRICi 18977500. VBIBacSub10457_2939.

Organism-specific databases

GenoListi BSU28120. [Micado ]

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OMAi RAIKPYP.
OrthoDBi EOG6QVRHN.
PhylomeDBi P30949.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci BSUB:BSU28120-MONOMER.

Miscellaneous databases

EvolutionaryTracei P30949.

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

« 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: September 3, 2014
This is version 116 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