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Protein

Histidine decarboxylase proenzyme

Gene

hdcA

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

Functioni

Catalytic activityi

L-histidine = histamine + CO2.

Cofactori

pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

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.
BRENDAi4.1.1.22. 2897.
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 – 97Combined sources
Turni10 – 123Combined sources
Beta strandi17 – 193Combined sources
Beta strandi21 – 233Combined sources
Beta strandi25 – 273Combined sources
Beta strandi34 – 363Combined sources
Beta strandi38 – 403Combined sources
Beta strandi43 – 508Combined sources
Helixi55 – 6511Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 713Combined sources
Beta strandi77 – 815Combined sources
Beta strandi89 – 913Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 973Combined sources
Helixi100 – 1045Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi118 – 1236Combined sources
Helixi125 – 13511Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi150 – 16213Combined sources
Turni170 – 1723Combined sources
Beta strandi175 – 18713Combined sources
Turni189 – 1913Combined sources
Beta strandi194 – 20310Combined sources
Helixi208 – 23326Combined sources
Beta strandi237 – 24812Combined sources
Beta strandi253 – 26715Combined sources
Helixi268 – 2703Combined sources
Helixi279 – 28810Combined sources
Helixi291 – 2988Combined sources
Turni305 – 3073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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.
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

        10         20         30         40         50
MSELDAKLNK LGVDRIAISP YKQWTRGYME PGNIGNGYVT GLKVDAGVRD
60 70 80 90 100
KSDDDVLDGI VSYDRAETKN AYIGQINMTT ASSFTGVQGR VIGYDILRSP
110 120 130 140 150
EVDKAKPLFT ETQWDGSELP IYDAKPLQDA LVEYFGTEQD RRHYPAPGSF
160 170 180 190 200
IVCANKGVTA ERPKNDADMK PGQGYGVWSA IAISFAKDPT KDSSMFVEDA
210 220 230 240 250
GVWETPNEDE LLEYLEGRRK AMAKSIAECG QDAHASFESS WIGFAYTMME
260 270 280 290 300
PGQIGNAITV APYVSLPIDS IPGGSILTPD KDMEIMENLT MPEWLEKMGY
310
KSLSANNALK Y
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:
EMBLi
GenBanki
DDBJi
Links Updated
J02613 Genomic DNA. Translation: AAB59151.1.
PIRiA25932. DCLBHP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02613 Genomic DNA. Translation: AAB59151.1.
PIRiA25932. DCLBHP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
SMRiP00862. Positions 2-82, 84-311.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14628.
BRENDAi4.1.1.22. 2897.
SABIO-RKP00862.

Miscellaneous databases

EvolutionaryTraceiP00862.

Family and domain databases

Gene3Di3.50.20.10. 1 hit.
4.10.510.10. 1 hit.
InterProiIPR003427. his_de-COase_proenz.
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.
ProtoNetiSearch...

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: April 1, 2015
This is version 102 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.