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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)DescriptionActionsGraphical viewLength
Binding sitei64Substrate1
Binding sitei82Substrate1
Active sitei198Proton donor1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000299532 – 82Histidine decarboxylase beta chainAdd BLAST81
ChainiPRO_000002995483 – 311Histidine decarboxylase alpha chainAdd BLAST229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei83Pyruvic acid (Ser)1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei82 – 83Cleavage (non-hydrolytic)2

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

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Turni10 – 12Combined sources3
Beta strandi17 – 19Combined sources3
Beta strandi21 – 23Combined sources3
Beta strandi25 – 27Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi43 – 50Combined sources8
Helixi55 – 65Combined sources11
Turni66 – 68Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi77 – 81Combined sources5
Beta strandi89 – 91Combined sources3
Turni92 – 94Combined sources3
Beta strandi95 – 97Combined sources3
Helixi100 – 104Combined sources5
Beta strandi108 – 112Combined sources5
Beta strandi118 – 123Combined sources6
Helixi125 – 135Combined sources11
Beta strandi138 – 141Combined sources4
Beta strandi150 – 162Combined sources13
Turni170 – 172Combined sources3
Beta strandi175 – 187Combined sources13
Turni189 – 191Combined sources3
Beta strandi194 – 203Combined sources10
Helixi208 – 233Combined sources26
Beta strandi237 – 248Combined sources12
Beta strandi253 – 267Combined sources15
Helixi268 – 270Combined sources3
Helixi279 – 288Combined sources10
Helixi291 – 298Combined sources8
Turni305 – 307Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti207N → D AA sequence (PubMed:6698997).Curated1
Sequence conflicti266L → I AA sequence (PubMed:6698997).Curated1
Sequence conflicti271I → L AA sequence (PubMed:6698997).Curated1
Sequence conflicti285 – 287Missing AA sequence (PubMed:6698997).Curated3

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
PDB 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.
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...

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: November 2, 2016
This is version 109 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

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 one 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.