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P00862 (DCHS_LACS3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine decarboxylase proenzyme
EC=4.1.1.22
Alternative name(s):
Pi chain

Cleaved into the following 2 chains:

  1. Histidine decarboxylase beta chain
  2. Histidine decarboxylase alpha chain
Gene names
Name:hdcA
OrganismLactobacillus sp. (strain 30a)
Taxonomic identifier1593 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-histidine = histamine + CO2.

Cofactor

Pyruvoyl group.

Subunit structure

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.

Ontologies

Keywords
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processhistidine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionhistidine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 8281Histidine decarboxylase beta chain
PRO_0000029953
Chain83 – 311229Histidine decarboxylase alpha chain
PRO_0000029954

Sites

Active site1981Proton donor
Binding site641Substrate
Binding site821Substrate
Site82 – 832Cleavage (non-hydrolytic)

Amino acid modifications

Modified residue831Pyruvic acid (Ser)

Experimental info

Sequence conflict2071N → D AA sequence Ref.3
Sequence conflict2661L → I AA sequence Ref.3
Sequence conflict2711I → L AA sequence Ref.3
Sequence conflict285 – 2873Missing AA sequence Ref.3

Secondary structure

1 ...................................................... 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00862 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D489583546578A0E

FASTA31134,233
        10         20         30         40         50         60 
MSELDAKLNK LGVDRIAISP YKQWTRGYME PGNIGNGYVT GLKVDAGVRD KSDDDVLDGI 

        70         80         90        100        110        120 
VSYDRAETKN AYIGQINMTT ASSFTGVQGR VIGYDILRSP EVDKAKPLFT ETQWDGSELP 

       130        140        150        160        170        180 
IYDAKPLQDA LVEYFGTEQD RRHYPAPGSF IVCANKGVTA ERPKNDADMK PGQGYGVWSA 

       190        200        210        220        230        240 
IAISFAKDPT KDSSMFVEDA GVWETPNEDE LLEYLEGRRK AMAKSIAECG QDAHASFESS 

       250        260        270        280        290        300 
WIGFAYTMME PGQIGNAITV APYVSLPIDS IPGGSILTPD KDMEIMENLT MPEWLEKMGY 

       310 
KSLSANNALK Y

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02613 Genomic DNA. Translation: AAB59151.1.
PIRDCLBHP. A25932.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQ6X-ray2.70A/C2-82[»]
B/D84-311[»]
1IBTX-ray2.60A/C/E2-81[»]
B/D/F84-310[»]
1IBUX-ray3.10A/C/E2-81[»]
B/D/F84-310[»]
1IBVX-ray2.50A/C/E2-81[»]
B/D/F84-310[»]
1IBWX-ray3.20A/C/E2-81[»]
B/D/F84-310[»]
1PYAX-ray2.50A/C/E2-82[»]
B/D/F84-311[»]
ProteinModelPortalP00862.
SMRP00862. Positions 2-82, 84-311.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14628.
SABIO-RKP00862.

Family and domain databases

Gene3D3.50.20.10. 1 hit.
4.10.510.10. 1 hit.
InterProIPR016106. Pyr-dep_his-deCO2ase_subdom.
IPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR016004. Pyr-dep_his_deCO2ase_PI_Gm-pos.
IPR003427. Pyruvoyl-dep_his_de-COase_PI.
[Graphical view]
PfamPF02329. HDC. 1 hit.
[Graphical view]
PIRSFPIRSF001341. His_decarboxylas. 1 hit.
ProDomPD024462. Pyruvoyl-dep_his_de-COase_PI. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56271. His_carbxylase. 1 hit.
TIGRFAMsTIGR00541. hisDCase_pyru. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00862.

Entry information

Entry nameDCHS_LACS3
AccessionPrimary (citable) accession number: P00862
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents