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P00862

- DCHS_LACS3

UniProt

P00862 - DCHS_LACS3

Protein

Histidine decarboxylase proenzyme

Gene

hdcA

Organism
Lactobacillus sp. (strain 30a)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-histidine = histamine + CO2.

    Cofactori

    Pyruvoyl group.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei64 – 641Substrate
    Sitei82 – 832Cleavage (non-hydrolytic)
    Binding sitei82 – 821Substrate
    Active sitei198 – 1981Proton donor

    GO - Molecular functioni

    1. histidine decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. histidine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Pyruvate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14628.
    SABIO-RKP00862.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine decarboxylase proenzyme (EC:4.1.1.22)
    Alternative name(s):
    Pi chain
    Cleaved into the following 2 chains:
    Gene namesi
    Name:hdcA
    OrganismiLactobacillus sp. (strain 30a)
    Taxonomic identifieri1593 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 8281Histidine decarboxylase beta chainPRO_0000029953Add
    BLAST
    Chaini83 – 311229Histidine decarboxylase alpha chainPRO_0000029954Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Pyruvic acid (Ser)

    Keywords - PTMi

    Zymogen

    Interactioni

    Subunit structurei

    The proenzyme is a hexamer of identical pi chains; each pi chain monomer is cleaved to form a small (or beta) chain and a large (or alpha) chain by non-hydrolytic self-catalysis.1 Publication

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Turni10 – 123
    Beta strandi17 – 193
    Beta strandi21 – 233
    Beta strandi25 – 273
    Beta strandi34 – 363
    Beta strandi38 – 403
    Beta strandi43 – 508
    Helixi55 – 6511
    Turni66 – 683
    Beta strandi69 – 713
    Beta strandi77 – 815
    Beta strandi89 – 913
    Turni92 – 943
    Beta strandi95 – 973
    Helixi100 – 1045
    Beta strandi108 – 1125
    Beta strandi118 – 1236
    Helixi125 – 13511
    Beta strandi138 – 1414
    Beta strandi150 – 16213
    Turni170 – 1723
    Beta strandi175 – 18713
    Turni189 – 1913
    Beta strandi194 – 20310
    Helixi208 – 23326
    Beta strandi237 – 24812
    Beta strandi253 – 26715
    Helixi268 – 2703
    Helixi279 – 28810
    Helixi291 – 2988
    Turni305 – 3073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HQ6X-ray2.70A/C2-82[»]
    B/D83-311[»]
    1IBTX-ray2.60A/C/E2-82[»]
    B/D/F83-311[»]
    1IBUX-ray3.10A/C/E2-82[»]
    B/D/F83-311[»]
    1IBVX-ray2.50A/C/E2-82[»]
    B/D/F84-311[»]
    1IBWX-ray3.20A/C/E2-82[»]
    B/D/F84-311[»]
    1PYAX-ray2.50A/C/E2-82[»]
    B/D/F84-311[»]
    ProteinModelPortaliP00862.
    SMRiP00862. Positions 2-82, 84-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00862.

    Family & Domainsi

    Family and domain databases

    Gene3Di3.50.20.10. 1 hit.
    4.10.510.10. 1 hit.
    InterProiIPR003427. his_de-COase_proenz.
    IPR016004. his_deCO2ase_Gm-pos.
    IPR016106. Pyr-dep_his-deCO2ase_subdom.
    IPR016104. Pyr-dep_his/arg-deCO2ase.
    IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
    [Graphical view]
    PfamiPF02329. HDC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001341. His_decarboxylas. 1 hit.
    ProDomiPD024462. Pyruvoyl-dep_his_de-COase_PI. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF56271. SSF56271. 1 hit.
    TIGRFAMsiTIGR00541. hisDCase_pyru. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P00862-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSELDAKLNK LGVDRIAISP YKQWTRGYME PGNIGNGYVT GLKVDAGVRD    50
    KSDDDVLDGI VSYDRAETKN AYIGQINMTT ASSFTGVQGR VIGYDILRSP 100
    EVDKAKPLFT ETQWDGSELP IYDAKPLQDA LVEYFGTEQD RRHYPAPGSF 150
    IVCANKGVTA ERPKNDADMK PGQGYGVWSA IAISFAKDPT KDSSMFVEDA 200
    GVWETPNEDE LLEYLEGRRK AMAKSIAECG QDAHASFESS WIGFAYTMME 250
    PGQIGNAITV APYVSLPIDS IPGGSILTPD KDMEIMENLT MPEWLEKMGY 300
    KSLSANNALK Y 311
    Length:311
    Mass (Da):34,233
    Last modified:January 23, 2007 - v2
    Checksum:iD489583546578A0E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071N → D AA sequence (PubMed:6698997)Curated
    Sequence conflicti266 – 2661L → I AA sequence (PubMed:6698997)Curated
    Sequence conflicti271 – 2711I → L AA sequence (PubMed:6698997)Curated
    Sequence conflicti285 – 2873Missing AA sequence (PubMed:6698997)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02613 Genomic DNA. Translation: AAB59151.1.
    PIRiA25932. DCLBHP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02613 Genomic DNA. Translation: AAB59151.1 .
    PIRi A25932. DCLBHP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HQ6 X-ray 2.70 A/C 2-82 [» ]
    B/D 83-311 [» ]
    1IBT X-ray 2.60 A/C/E 2-82 [» ]
    B/D/F 83-311 [» ]
    1IBU X-ray 3.10 A/C/E 2-82 [» ]
    B/D/F 83-311 [» ]
    1IBV X-ray 2.50 A/C/E 2-82 [» ]
    B/D/F 84-311 [» ]
    1IBW X-ray 3.20 A/C/E 2-82 [» ]
    B/D/F 84-311 [» ]
    1PYA X-ray 2.50 A/C/E 2-82 [» ]
    B/D/F 84-311 [» ]
    ProteinModelPortali P00862.
    SMRi P00862. Positions 2-82, 84-311.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14628.
    SABIO-RK P00862.

    Miscellaneous databases

    EvolutionaryTracei P00862.

    Family and domain databases

    Gene3Di 3.50.20.10. 1 hit.
    4.10.510.10. 1 hit.
    InterProi IPR003427. his_de-COase_proenz.
    IPR016004. his_deCO2ase_Gm-pos.
    IPR016106. Pyr-dep_his-deCO2ase_subdom.
    IPR016104. Pyr-dep_his/arg-deCO2ase.
    IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
    [Graphical view ]
    Pfami PF02329. HDC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001341. His_decarboxylas. 1 hit.
    ProDomi PD024462. Pyruvoyl-dep_his_de-COase_PI. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF56271. SSF56271. 1 hit.
    TIGRFAMsi TIGR00541. hisDCase_pyru. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of wild type and a mutant histidine decarboxylase from Lactobacillus 30a."
      Vanderslice P., Copeland W.C., Robertus J.D.
      J. Biol. Chem. 261:15186-15191(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Histidine decarboxylase of Lactobacillus 30a. Comparative sequences of the beta chain from wild type and mutant enzymes."
      Vaaler G.L., Recsei P.A., Fox J.L., Snell E.E.
      J. Biol. Chem. 257:12770-12774(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-82.
    3. "Histidine decarboxylase of Lactobacillus 30a. Sequences of the overlapping peptides, the complete alpha chain, and prohistidine decarboxylase."
      Huynh Q.K., Recsei P.A., Vaaler G.L., Snell E.E.
      J. Biol. Chem. 259:2833-2839(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 83-308, PYRUVATE FORMATION AT SER-83.
    4. "Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0-A resolution."
      Parks E.H., Ernst S.R., Hamlin R., Xuong N.G., Hackert M.L.
      J. Mol. Biol. 182:455-465(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    5. "Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis."
      Gallagher T., Snell E.E., Hackert M.L.
      J. Biol. Chem. 264:12737-12743(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBSTRATE BINDING AT ASP-64 AND SER-82.
    6. "Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a."
      Gallagher T., Rozwarski D.A., Ernst S.R., Hackert M.L.
      J. Mol. Biol. 230:516-528(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    7. "pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a."
      Schelp E., Worley S., Monzingo A.F., Ernst S., Robertus J.D.
      J. Mol. Biol. 306:727-732(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

    Entry informationi

    Entry nameiDCHS_LACS3
    AccessioniPrimary (citable) accession number: P00862
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 99 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3