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UniProtKB/Swiss-Prot entry P30950


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HEM2_BACSU
Primary accession number P30950
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Delta-aminolevulinic acid dehydratase
Synonyms ALADH
ALAD
EC 4.2.1.24
Porphobilinogen synthase
Gene name
Name: hemB
OrderedLocusNames: BSU28130
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1672867 [NCBI, ExPASy, EBI, Israel, Japan]
Hansson M., Rutberg L., Schroeder I., Hederstedt L.;
"The Bacillus subtilis hemAXCDBL gene cluster, which encodes enzymes of the biosynthetic pathway from glutamate to uroporphyrinogen III.";
J. Bacteriol. 173:2590-2599(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57676; AAA22514.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14773.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C42728; C42728.
RefSeq NP_390691.1; -.
3D structure databases
HSSP Q59643; 1B4K. [HSSP ENTRY / PDB]
ModBase P30950.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2809-MON; -.
Organism-specific databases
SubtiList BG10344; hemB. [Micado]
Ontologies
GO
GO:0004655; Molecular function: porphobilinogen synthase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006779; Biological process: porphyrin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11458; AlaD_dehydratase; 1.
Pfam PF00490; ALAD; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001415; Porphbilin_synth; 1.
PRINTS PR00144; DALDHYDRTASE.
ProDom PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00169; D_ALA_DEHYDRATASE; 1.
BLOCKS P30950.
ProtoNet P30950.
Genome annotation databases
GeneID 936972; -.
GenomeReviews AL009126_GR; BSU28130.
KEGG bsu:BSU28130; -.
NMPDR fig|224308.1.peg.2816; -.
Phylogenomic databases
HOGENOM P30950; -.
Genome annotation databases
CMR P30950; BSU28130.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Lyase; Porphyrin biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   324  324     Delta-aminolevulinic acid dehydratase. PRO_0000140493
REGION   117   135  19     Zinc-binding (By similarity). 
ACT_SITE   248   248        By similarity. 
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 36209 Da [This is the MW of the unprocessed precursor] CRC64: C1CF7E157AE6CB07 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQSFNRHRR LRTSKAMREM VKETRLHPSD FIYPIFVVEG LEGKKAVPSM PDVHHVSLDL 

        70         80         90        100        110        120 
LKDEVAELVK LGIQSVIVFG IPEEKDDCGT QAYHDHGIVQ KAITEIKEHF PEMVVVADTC 

       130        140        150        160        170        180 
LCEYTDHGHC GLVKDGVILN DESLELLAQT AVSQAKAGAD IIAPSNMMDG FVTVIREALD 

       190        200        210        220        230        240 
KEGFVNIPIM SYAVKYSSEF YGPFRDAANS TPQFGDRKTY QMDPANRMEA LREAQSDVEE 

       250        260        270        280        290        300 
GADFLIVKPS LSYMDIMRDV KNEFTLPLVA YNVSGEYSMV KAAAQNGWIK EKEIVLEILT 

       310        320 
SMKRAGADLI ITYHAKDAAK WLAE 

P30950 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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