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P28629

- ADIA_ECOLI

UniProt

P28629 - ADIA_ECOLI

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Protein
Biodegradative arginine decarboxylase
Gene
adiA, adi, b4117, JW5731
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. arginine decarboxylase activity Source: EcoCyc
  2. pyridoxal phosphate binding Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. arginine catabolic process Source: EcoliWiki
  2. intracellular pH elevation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ARGDECARBOXDEG-MONOMER.
ECOL316407:JW5731-MONOMER.
MetaCyc:ARGDECARBOXDEG-MONOMER.
BRENDAi4.1.1.19. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Biodegradative arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:adiA
Synonyms:adi
Ordered Locus Names:b4117, JW5731
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11501. adiA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 755755Biodegradative arginine decarboxylase
PRO_0000201149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei386 – 3861N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP28629.
PRIDEiP28629.

Expressioni

Inductioni

Under conditions of acidic pH, anaerobiosis and rich medium.

Gene expression databases

GenevestigatoriP28629.

Interactioni

Subunit structurei

Homodecamer.

Protein-protein interaction databases

DIPiDIP-2903N.
IntActiP28629. 6 interactions.
MINTiMINT-1241522.
STRINGi511145.b4117.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi15 – 3016
Beta strandi34 – 407
Helixi41 – 488
Turni49 – 513
Beta strandi55 – 606
Helixi66 – 8217
Beta strandi88 – 925
Helixi94 – 996
Helixi103 – 1086
Beta strandi110 – 1145
Turni115 – 1173
Helixi120 – 13617
Helixi141 – 15010
Beta strandi156 – 1605
Turni161 – 1666
Helixi167 – 1704
Helixi172 – 18110
Helixi183 – 1875
Turni194 – 1974
Turni200 – 2034
Helixi205 – 21814
Beta strandi221 – 2288
Helixi229 – 24113
Beta strandi247 – 2537
Helixi256 – 26510
Beta strandi268 – 2725
Helixi287 – 2904
Helixi292 – 30110
Turni303 – 3053
Helixi306 – 3083
Beta strandi316 – 3216
Beta strandi325 – 3284
Helixi330 – 3378
Turni338 – 3403
Beta strandi342 – 3476
Helixi354 – 3563
Helixi358 – 3603
Beta strandi363 – 3664
Beta strandi374 – 38310
Turni384 – 3863
Beta strandi387 – 3893
Beta strandi395 – 4006
Helixi408 – 41710
Helixi425 – 43814
Helixi441 – 46929
Turni470 – 4723
Beta strandi477 – 4804
Beta strandi482 – 4854
Turni487 – 4893
Beta strandi492 – 4943
Helixi495 – 4973
Helixi500 – 5056
Helixi507 – 5093
Turni517 – 5193
Beta strandi528 – 5314
Beta strandi535 – 5395
Beta strandi547 – 5493
Helixi556 – 5649
Turni565 – 5673
Beta strandi571 – 5733
Beta strandi575 – 5817
Turni588 – 5914
Helixi592 – 60716
Helixi611 – 6144
Helixi616 – 6216
Turni623 – 6253
Helixi631 – 64515
Helixi647 – 65610
Beta strandi661 – 6633
Helixi665 – 6739
Beta strandi677 – 6815
Helixi682 – 6843
Beta strandi689 – 6924
Beta strandi694 – 6963
Turni697 – 6993
Helixi716 – 73015
Beta strandi741 – 7444
Beta strandi747 – 7537

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYCX-ray2.40A/B/C/D/E/F/G/H/I/J1-755[»]
ProteinModelPortaliP28629.

Miscellaneous databases

EvolutionaryTraceiP28629.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1982.
HOGENOMiHOG000164394.
KOiK01584.
OMAiANDWVEC.
OrthoDBiEOG696BRZ.
PhylomeDBiP28629.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.100.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR005308. OKR_de-COase_N.
IPR011193. Orn/lys/arg_de-COase.
IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
IPR008286. Prn/Lys/Arg_de-COase_C.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01276. OKR_DC_1. 1 hit.
PF03711. OKR_DC_1_C. 1 hit.
PF03709. OKR_DC_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF009393. Orn_decarb. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
SSF55904. SSF55904. 1 hit.
PROSITEiPS00703. OKR_DC_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28629-1 [UniParc]FASTAAdd to Basket

« Hide

MKVLIVESEF LHQDTWVGNA VERLADALSQ QNVTVIKSTS FDDGFAILSS    50
NEAIDCLMFS YQMEHPDEHQ NVRQLIGKLH ERQQNVPVFL LGDREKALAA 100
MDRDLLELVD EFAWILEDTA DFIAGRAVAA MTRYRQQLLP PLFSALMKYS 150
DIHEYSWAAP GHQGGVGFTK TPAGRFYHDY YGENLFRTDM GIERTSLGSL 200
LDHTGAFGES EKYAARVFGA DRSWSVVVGT SGSNRTIMQA CMTDNDVVVV 250
DRNCHKSIEQ GLMLTGAKPV YMVPSRNRYG IIGPIYPQEM QPETLQKKIS 300
ESPLTKDKAG QKPSYCVVTN CTYDGVCYNA KEAQDLLEKT SDRLHFDEAW 350
YGYARFNPIY ADHYAMRGEP GDHNGPTVFA THSTHKLLNA LSQASYIHVR 400
EGRGAINFSR FNQAYMMHAT TSPLYAICAS NDVAVSMMDG NSGLSLTQEV 450
IDEAVDFRQA MARLYKEFTA DGSWFFKPWN KEVVTDPQTG KTYDFADAPT 500
KLLTTVQDCW VMHPGESWHG FKDIPDNWSM LDPIKVSILA PGMGEDGELE 550
ETGVPAALVT AWLGRHGIVP TRTTDFQIMF LFSMGVTRGK WGTLVNTLCS 600
FKRHYDANTP LAQVMPELVE QYPDTYANMG IHDLGDTMFA WLKENNPGAR 650
LNEAYSGLPV AEVTPREAYN AIVDNNVELV SIENLPGRIA ANSVIPYPPG 700
IPMLLSGENF GDKNSPQVSY LRSLQSWDHH FPGFEHETEG TEIIDGIYHV 750
MCVKA 755
Length:755
Mass (Da):84,425
Last modified:December 1, 1992 - v1
Checksum:i0FCB715144649F8F
GO

Sequence cautioni

The sequence AAA97017.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAE78119.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751L → P1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93362 Genomic DNA. Translation: AAA23481.1.
U14003 Genomic DNA. Translation: AAA97017.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77078.2.
AP009048 Genomic DNA. Translation: BAE78119.1. Different initiation.
M18425 Genomic DNA. No translation available.
PIRiS56346.
RefSeqiNP_418541.2. NC_000913.3.
YP_492260.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77078; AAC77078; b4117.
BAE78119; BAE78119; BAE78119.
GeneIDi12934085.
948638.
KEGGiecj:Y75_p4004.
eco:b4117.
PATRICi32123799. VBIEscCol129921_4248.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93362 Genomic DNA. Translation: AAA23481.1 .
U14003 Genomic DNA. Translation: AAA97017.1 . Different initiation.
U00096 Genomic DNA. Translation: AAC77078.2 .
AP009048 Genomic DNA. Translation: BAE78119.1 . Different initiation.
M18425 Genomic DNA. No translation available.
PIRi S56346.
RefSeqi NP_418541.2. NC_000913.3.
YP_492260.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VYC X-ray 2.40 A/B/C/D/E/F/G/H/I/J 1-755 [» ]
ProteinModelPortali P28629.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-2903N.
IntActi P28629. 6 interactions.
MINTi MINT-1241522.
STRINGi 511145.b4117.

Proteomic databases

PaxDbi P28629.
PRIDEi P28629.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77078 ; AAC77078 ; b4117 .
BAE78119 ; BAE78119 ; BAE78119 .
GeneIDi 12934085.
948638.
KEGGi ecj:Y75_p4004.
eco:b4117.
PATRICi 32123799. VBIEscCol129921_4248.

Organism-specific databases

EchoBASEi EB1464.
EcoGenei EG11501. adiA.

Phylogenomic databases

eggNOGi COG1982.
HOGENOMi HOG000164394.
KOi K01584.
OMAi ANDWVEC.
OrthoDBi EOG696BRZ.
PhylomeDBi P28629.

Enzyme and pathway databases

BioCyci EcoCyc:ARGDECARBOXDEG-MONOMER.
ECOL316407:JW5731-MONOMER.
MetaCyc:ARGDECARBOXDEG-MONOMER.
BRENDAi 4.1.1.19. 2026.

Miscellaneous databases

EvolutionaryTracei P28629.
PROi P28629.

Gene expression databases

Genevestigatori P28629.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.100.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR005308. OKR_de-COase_N.
IPR011193. Orn/lys/arg_de-COase.
IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
IPR008286. Prn/Lys/Arg_de-COase_C.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF01276. OKR_DC_1. 1 hit.
PF03711. OKR_DC_1_C. 1 hit.
PF03709. OKR_DC_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF009393. Orn_decarb. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
SSF55904. SSF55904. 1 hit.
PROSITEi PS00703. OKR_DC_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli."
    Stim K.P., Bennett G.N.
    J. Bacteriol. 175:1221-1234(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Organisation of the regulatory region of the Escherichia coli melibiose operon."
    Webster C., Kempsell K., Booth I., Busby S.
    Gene 59:253-263(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
  6. "Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site."
    Sabo D.L., Fischer E.H.
    Biochemistry 13:670-676(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7.
    Strain: B.

Entry informationi

Entry nameiADIA_ECOLI
AccessioniPrimary (citable) accession number: P28629
Secondary accession number(s): P78138, Q2M6I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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