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P00862

- DCHS_LACS3

UniProt

P00862 - DCHS_LACS3

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Protein

Histidine decarboxylase proenzyme

Gene
hdcA
Organism
Lactobacillus sp. (strain 30a)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071N → D AA sequence 1 Publication
Sequence conflicti266 – 2661L → I AA sequence 1 Publication
Sequence conflicti271 – 2711I → L AA sequence 1 Publication
Sequence conflicti285 – 2873Missing AA sequence 1 Publication

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: September 3, 2014
This is version 98 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

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