Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P18079

- HEM1_RHOCB

UniProt

P18079 - HEM1_RHOCB

Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Substrate
    Binding sitei137 – 1371Substrate
    Binding sitei156 – 1561Substrate
    Binding sitei189 – 1891Pyridoxal phosphate
    Binding sitei217 – 2171Pyridoxal phosphate
    Binding sitei245 – 2451Pyridoxal phosphate
    Active sitei248 – 24811 Publication
    Binding sitei277 – 2771Pyridoxal phosphate
    Binding sitei278 – 2781Pyridoxal phosphate
    Binding sitei365 – 3651Substrate

    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

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Heme biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciRCAP272942:GJIY-1471-MONOMER.
    RETL1328306-WGS:GSTH-5523-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:RCAP_rcc01447
    OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
    Taxonomic identifieri272942 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    ProteomesiUP000002361: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4094095-aminolevulinate synthasePRO_0000163828Add
    BLAST

    Amino acid modifications

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

    Structurei

    Secondary structure

    1
    409
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Beta strandi25 – 284
    Beta strandi35 – 395
    Beta strandi45 – 506
    Helixi59 – 613
    Helixi63 – 7614
    Turni84 – 863
    Helixi91 – 10313
    Beta strandi107 – 1137
    Helixi115 – 12915
    Beta strandi134 – 1385
    Helixi143 – 1519
    Beta strandi156 – 1594
    Helixi164 – 17310
    Beta strandi180 – 1878
    Turni189 – 1913
    Helixi197 – 20711
    Beta strandi210 – 2145
    Turni216 – 2216
    Helixi229 – 2335
    Helixi236 – 2383
    Beta strandi240 – 2489
    Beta strandi255 – 2595
    Helixi261 – 27010
    Helixi272 – 2754
    Helixi282 – 29514
    Helixi298 – 32124
    Beta strandi329 – 3313
    Beta strandi333 – 3364
    Helixi340 – 35415
    Turni363 – 3653
    Beta strandi372 – 3754
    Helixi383 – 39614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BWNX-ray2.10A/B/D/E1-401[»]
    2BWOX-ray2.80A/B/D/E1-401[»]
    2BWPX-ray2.70A/B/D/E1-401[»]
    ProteinModelPortaliP18079.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18079.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000221020.
    KOiK00643.
    OMAiVMDSTTH.

    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.

    P18079-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYNLALDKA IQKLHDEGRY RTFIDIEREK GAFPKAQWNR PDGGKQDITV    50
    WCGNDYLGMG QHPVVLAAMH EALEAVGAGS GGTRNISGTT AYHRRLEAEI 100
    ADLHGKEAAL VFSSAYIAND ATLSTLRVLF PGLIIYSDSL NHASMIEGIK 150
    RNAGPKRIFR HNDVAHLREL IAADDPAAPK LIAFESVYSM DGDFGPIKEI 200
    CDIADEFGAL TYIDEVHAVG MYGPRGAGVA ERDGLMHRID IFNGTLAKAY 250
    GVFGGYIAAS AKMVDAVRSY APGFIFSTSL PPAIAAGAQA SIAFLKTAEG 300
    QKLRDAQQMH AKVLKMRLKA LGMPIIDHGS HIVPVVIGDP VHTKAVSDML 350
    LSDYGVYVQP INFPTVPRGT ERLRFTPSPV HDLKQIDGLV HAMDLLWARC 400
    ALNRAEASA 409
    Length:409
    Mass (Da):44,374
    Last modified:May 31, 2011 - v2
    Checksum:iFCC89DA6EBA8DFB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281V → L in CAA37857. (PubMed:2381418)Curated
    Sequence conflicti128 – 1281V → L in CAA37393. (PubMed:1904045)Curated
    Sequence conflicti402 – 4098Missing in CAA37857. (PubMed:2381418)Curated
    Sequence conflicti402 – 4098Missing in CAA37393. (PubMed:1904045)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53309 Genomic DNA. Translation: CAA37393.1.
    X53864 Genomic DNA. Translation: CAA37857.1.
    CP001312 Genomic DNA. Translation: ADE85192.1.
    PIRiS10528.
    RefSeqiYP_003577599.1. NC_014034.1.

    Genome annotation databases

    EnsemblBacteriaiADE85192; ADE85192; RCAP_rcc01447.
    GeneIDi9004270.
    KEGGircp:RCAP_rcc01447.
    PATRICi35502998. VBIRhoCap134200_1459.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53309 Genomic DNA. Translation: CAA37393.1 .
    X53864 Genomic DNA. Translation: CAA37857.1 .
    CP001312 Genomic DNA. Translation: ADE85192.1 .
    PIRi S10528.
    RefSeqi YP_003577599.1. NC_014034.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BWN X-ray 2.10 A/B/D/E 1-401 [» ]
    2BWO X-ray 2.80 A/B/D/E 1-401 [» ]
    2BWP X-ray 2.70 A/B/D/E 1-401 [» ]
    ProteinModelPortali P18079.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADE85192 ; ADE85192 ; RCAP_rcc01447 .
    GeneIDi 9004270.
    KEGGi rcp:RCAP_rcc01447.
    PATRICi 35502998. VBIRhoCap134200_1459.

    Phylogenomic databases

    HOGENOMi HOG000221020.
    KOi K00643.
    OMAi VMDSTTH.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00375 .
    BioCyci RCAP272942:GJIY-1471-MONOMER.
    RETL1328306-WGS:GSTH-5523-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P18079.

    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

    1. "Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a delta-aminolevulinic acid-dependent mutant strain."
      Hornberger U., Liebetanz R., Tichy H.V., Drews G.
      Mol. Gen. Genet. 221:371-378(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
    2. "Use of a lacZ fusion to study transcriptional regulation of the Rhodobacter capsulatus hemA gene."
      Wright M.S., Eckert J.J., Biel S.W., Biel A.J.
      FEMS Microbiol. Lett. 62:339-342(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
    3. "Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
      Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
      J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
    4. "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans."
      Astner I., Schulze J.O., van den Heuvel J., Jahn D., Schubert W.D., Heinz D.W.
      EMBO J. 24:3166-3177(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-401, SUBUNIT, COFACTOR-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE.

    Entry informationi

    Entry nameiHEM1_RHOCB
    AccessioniPrimary (citable) accession number: P18079
    Secondary accession number(s): D5AT85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 103 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3