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P38092

- HEM1_EMENI

UniProt

P38092 - HEM1_EMENI

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Protein
5-aminolevulinate synthase, mitochondrial
Gene
hemA, AN2284
Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei170 – 1701Substrate By similarity
Binding sitei283 – 2831Substrate By similarity
Binding sitei302 – 3021Substrate By similarity
Binding sitei335 – 3351Pyridoxal phosphate By similarity
Binding sitei363 – 3631Pyridoxal phosphate By similarity
Binding sitei409 – 4091Pyridoxal phosphate By similarity
Active sitei412 – 4121 By similarity
Binding sitei441 – 4411Pyridoxal phosphate By similarity
Binding sitei442 – 4421Pyridoxal phosphate By similarity
Binding sitei527 – 5271Substrate By similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro
  3. serine C-palmitoyltransferase activity Source: ASPGD

GO - Biological processi

  1. biotin biosynthetic process Source: ASPGD
  2. establishment of cell polarity Source: ASPGD
  3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  4. sphingolipid biosynthetic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, mitochondrial (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
ORF Names:AN2284
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. peroxisome Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 6485-aminolevulinate synthase, mitochondrialPRO_0000001240
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei412 – 4121N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00008976.

Structurei

3D structure databases

ProteinModelPortaliP38092.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
KOiK00643.
OMAiKLAQYPK.
OrthoDBiEOG7HHX1P.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38092-1 [UniParc]FASTAAdd to Basket

« Hide

MEALLQQSRA MCPFLKRSSP NTLRSLATAT RPSTSPGGGT MTNLQRIARR    50
CPVMSKALAV QSARMTGTKR FTSSAAGVPG AGAGTPKPTR GSPGKRALHS 100
TGGNGANMST EFHKGAQQIH PGLSNATRSH VGASATVSGP TPRAPVAAPF 150
DYDAFYNAEL QKKHQDKSYR YFNNINRLAQ EFPRAHTASK DEKVTVWCSN 200
DYLGMGRNPE VLATMHKTLD TYGAGAGGTR NISGHNQHAV SLENTLAKLH 250
GKEAALVFSS CFVANDATLA TLGSKMPDCV ILSDSLNHAS MIQGIRHSGA 300
KKMVFKHNDL VDLETKLASL PLHVPKIIAF ESVYSMCGSI APIEAICDLA 350
DKYGAITFLD EVHAVGMYGP HGAGVAEHLD YEIYASQDTA NPLSTKGTVM 400
DRINIITGTL GKAYGCVGGY IAGSAALVDT IRSLAPGFIF TTSLPPATMA 450
GADTAIRYQA RHQQDRILQQ LHTRAVKQSF KDLDIPVIPN PSHIVPLLVG 500
DAELAKQASD KLLEEHGIYV QAINYPTVPR GEERLRITPT PGHTQELRDH 550
LVEAVNTVWN DLGIKRASDW KAMGGFVGVG VEAAELENQP IWTDAQLNMR 600
PDETLEAAVE REFQAAVPGM KAGGAKAKPV GSIAANPIGA SIPVAAAA 648
Length:648
Mass (Da):68,960
Last modified:May 26, 2009 - v2
Checksum:i1D450D773925F13F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001A → R in CAA45508. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64170 Genomic DNA. Translation: CAA45508.1.
AACD01000038 Genomic DNA. Translation: EAA64395.1.
BN001307 Genomic DNA. Translation: CBF86531.1.
PIRiS31846.
RefSeqiXP_659888.1. XM_654796.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008976; CADANIAP00008976; CADANIAG00008976.
GeneIDi2874789.
KEGGiani:AN2284.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64170 Genomic DNA. Translation: CAA45508.1 .
AACD01000038 Genomic DNA. Translation: EAA64395.1 .
BN001307 Genomic DNA. Translation: CBF86531.1 .
PIRi S31846.
RefSeqi XP_659888.1. XM_654796.1.

3D structure databases

ProteinModelPortali P38092.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00008976.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008976 ; CADANIAP00008976 ; CADANIAG00008976 .
GeneIDi 2874789.
KEGGi ani:AN2284.2.

Phylogenomic databases

eggNOGi COG0156.
HOGENOMi HOG000221020.
KOi K00643.
OMAi KLAQYPK.
OrthoDBi EOG7HHX1P.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01821. 5aminolev_synth. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and nucleotide sequence of the 5-aminolevulinate synthase gene from Aspergillus nidulans."
    Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M.
    Curr. Genet. 23:501-507(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R153.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiHEM1_EMENI
AccessioniPrimary (citable) accession number: P38092
Secondary accession number(s): C8VN31, Q5BAZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: January 22, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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