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P43089

- HEM1_PARDP

UniProt

P43089 - HEM1_PARDP

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Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei189 – 1891Pyridoxal phosphateBy similarity
Binding sitei217 – 2171Pyridoxal phosphateBy similarity
Binding sitei245 – 2451Pyridoxal phosphateBy similarity
Active sitei248 – 2481By similarity
Binding sitei277 – 2771Pyridoxal phosphateBy similarity
Binding sitei278 – 2781Pyridoxal phosphateBy similarity
Binding sitei365 – 3651SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-1848-MONOMER.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
Ordered Locus Names:Pden_1822
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4094095-aminolevulinate synthasePRO_0000163826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineCurated

Interactioni

Protein-protein interaction databases

STRINGi318586.Pden_1822.

Structurei

3D structure databases

ProteinModelPortaliP43089.
SMRiP43089. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
KOiK00643.
OrthoDBiEOG6Q8HZD.

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.

P43089-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDYSAALDQA IGKLHEEGRY RTFIDIERRK GAYPQAVWTR PDGTETRITV
60 70 80 90 100
WCGNDYLGMG QHPVVLAAMH EALDATGAGS GGTRNISGTT VYHKRLEAEL
110 120 130 140 150
SDLHGKEAAL VFSSAYIAND ATLSTLRKLF PGLIIYSDEL NHASMIEGIK
160 170 180 190 200
RFDGAKRIFR HNDVAHLREL LAADDPEAPK LIAFESIYSM DGDFGPIKAI
210 220 230 240 250
CDLADEFNAL TYLDEVHAVG MYGPRGGGVA ERDGLSHRID IFNGTLGKAF
260 270 280 290 300
GVFGGYIAAS ARMVDAIRSY APGFIFTTSL PPAVAAGAAA SIAFLKTAEG
310 320 330 340 350
QLLRDQQQLN ARILKMRLRG LGMPIMDHGS HIVPVHVGNP VHCKALSDML
360 370 380 390 400
LADFGIYVQP INFPTVPRGT ERLRFTPSPV HDPKQIDHLV KAMDSLWSQC

KLNRSTSAA
Length:409
Mass (Da):44,560
Last modified:March 6, 2007 - v2
Checksum:i1A2EEE178D58B32E
GO

Sequence cautioni

The sequence ABL69919.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351Q → T in AAA62279. (PubMed:7928952)Curated
Sequence conflicti101 – 1011S → A in AAA62279. (PubMed:7928952)Curated
Sequence conflicti115 – 1151A → V in AAA62279. (PubMed:7928952)Curated
Sequence conflicti152 – 1554FDGA → STAP in AAA62279. (PubMed:7928952)Curated
Sequence conflicti165 – 1651A → G in AAA62279. (PubMed:7928952)Curated
Sequence conflicti195 – 1951G → A in AAA62279. (PubMed:7928952)Curated
Sequence conflicti199 – 1991A → E in AAA62279. (PubMed:7928952)Curated
Sequence conflicti247 – 2471G → A in AAA62279. (PubMed:7928952)Curated
Sequence conflicti258 – 2603AAS → GFG in AAA62279. (PubMed:7928952)Curated
Sequence conflicti288 – 2881A → V in AAA62279. (PubMed:7928952)Curated
Sequence conflicti302 – 3032LL → FV in AAA62279. (PubMed:7928952)Curated
Sequence conflicti311 – 3133ARI → GRL in AAA62279. (PubMed:7928952)Curated
Sequence conflicti321 – 3211L → A in AAA62279. (PubMed:7928952)Curated
Sequence conflicti325 – 3251I → V in AAA62279. (PubMed:7928952)Curated
Sequence conflicti355 – 3551G → S in AAA62279. (PubMed:7928952)Curated
Sequence conflicti377 – 3771P → A in AAA62279. (PubMed:7928952)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12508 Genomic DNA. Translation: AAA62279.1.
CP000489 Genomic DNA. Translation: ABL69919.1. Different initiation.
RefSeqiYP_915615.1. NC_008686.1.

Genome annotation databases

EnsemblBacteriaiABL69919; ABL69919; Pden_1822.
GeneIDi4578534.
KEGGipde:Pden_1822.
PATRICi22854745. VBIParDen97112_1755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12508 Genomic DNA. Translation: AAA62279.1 .
CP000489 Genomic DNA. Translation: ABL69919.1 . Different initiation.
RefSeqi YP_915615.1. NC_008686.1.

3D structure databases

ProteinModelPortali P43089.
SMRi P43089. Positions 1-397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 318586.Pden_1822.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL69919 ; ABL69919 ; Pden_1822 .
GeneIDi 4578534.
KEGGi pde:Pden_1822.
PATRICi 22854745. VBIParDen97112_1755.

Phylogenomic databases

eggNOGi COG0156.
HOGENOMi HOG000221020.
KOi K00643.
OrthoDBi EOG6Q8HZD.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .
BioCyci PDEN318586:GCVQ-1848-MONOMER.

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. "Differential reduction in soluble and membrane-bound c-type cytochrome contents in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase activity."
    Page M.D., Ferguson S.J.
    J. Bacteriol. 176:5919-5928(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pd 1222.

Entry informationi

Entry nameiHEM1_PARDP
AccessioniPrimary (citable) accession number: P43089
Secondary accession number(s): A1B325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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