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P28629

- ADIA_ECOLI

UniProt

P28629 - ADIA_ECOLI

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Protein

Biodegradative arginine decarboxylase

Gene

adiA

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

GO - Molecular functioni

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

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 decarboxylasePRO_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

1
755
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi15 – 3016Combined sources
Beta strandi34 – 407Combined sources
Helixi41 – 488Combined sources
Turni49 – 513Combined sources
Beta strandi55 – 606Combined sources
Helixi66 – 8217Combined sources
Beta strandi88 – 925Combined sources
Helixi94 – 996Combined sources
Helixi103 – 1086Combined sources
Beta strandi110 – 1145Combined sources
Turni115 – 1173Combined sources
Helixi120 – 13617Combined sources
Helixi141 – 15010Combined sources
Beta strandi156 – 1605Combined sources
Turni161 – 1666Combined sources
Helixi167 – 1704Combined sources
Helixi172 – 18110Combined sources
Helixi183 – 1875Combined sources
Turni194 – 1974Combined sources
Turni200 – 2034Combined sources
Helixi205 – 21814Combined sources
Beta strandi221 – 2288Combined sources
Helixi229 – 24113Combined sources
Beta strandi247 – 2537Combined sources
Helixi256 – 26510Combined sources
Beta strandi268 – 2725Combined sources
Helixi287 – 2904Combined sources
Helixi292 – 30110Combined sources
Turni303 – 3053Combined sources
Helixi306 – 3083Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi325 – 3284Combined sources
Helixi330 – 3378Combined sources
Turni338 – 3403Combined sources
Beta strandi342 – 3476Combined sources
Helixi354 – 3563Combined sources
Helixi358 – 3603Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi374 – 38310Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3893Combined sources
Beta strandi395 – 4006Combined sources
Helixi408 – 41710Combined sources
Helixi425 – 43814Combined sources
Helixi441 – 46929Combined sources
Turni470 – 4723Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi482 – 4854Combined sources
Turni487 – 4893Combined sources
Beta strandi492 – 4943Combined sources
Helixi495 – 4973Combined sources
Helixi500 – 5056Combined sources
Helixi507 – 5093Combined sources
Turni517 – 5193Combined sources
Beta strandi528 – 5314Combined sources
Beta strandi535 – 5395Combined sources
Beta strandi547 – 5493Combined sources
Helixi556 – 5649Combined sources
Turni565 – 5673Combined sources
Beta strandi571 – 5733Combined sources
Beta strandi575 – 5817Combined sources
Turni588 – 5914Combined sources
Helixi592 – 60716Combined sources
Helixi611 – 6144Combined sources
Helixi616 – 6216Combined sources
Turni623 – 6253Combined sources
Helixi631 – 64515Combined sources
Helixi647 – 65610Combined sources
Beta strandi661 – 6633Combined sources
Helixi665 – 6739Combined sources
Beta strandi677 – 6815Combined sources
Helixi682 – 6843Combined sources
Beta strandi689 – 6924Combined sources
Beta strandi694 – 6963Combined sources
Turni697 – 6993Combined sources
Helixi716 – 73015Combined sources
Beta strandi741 – 7444Combined sources
Beta strandi747 – 7537Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYCX-ray2.40A/B/C/D/E/F/G/H/I/J1-755[»]
ProteinModelPortaliP28629.
SMRiP28629. Positions 1-755.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28629.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1982.
HOGENOMiHOG000164394.
InParanoidiP28629.
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

        10         20         30         40         50
MKVLIVESEF LHQDTWVGNA VERLADALSQ QNVTVIKSTS FDDGFAILSS
60 70 80 90 100
NEAIDCLMFS YQMEHPDEHQ NVRQLIGKLH ERQQNVPVFL LGDREKALAA
110 120 130 140 150
MDRDLLELVD EFAWILEDTA DFIAGRAVAA MTRYRQQLLP PLFSALMKYS
160 170 180 190 200
DIHEYSWAAP GHQGGVGFTK TPAGRFYHDY YGENLFRTDM GIERTSLGSL
210 220 230 240 250
LDHTGAFGES EKYAARVFGA DRSWSVVVGT SGSNRTIMQA CMTDNDVVVV
260 270 280 290 300
DRNCHKSIEQ GLMLTGAKPV YMVPSRNRYG IIGPIYPQEM QPETLQKKIS
310 320 330 340 350
ESPLTKDKAG QKPSYCVVTN CTYDGVCYNA KEAQDLLEKT SDRLHFDEAW
360 370 380 390 400
YGYARFNPIY ADHYAMRGEP GDHNGPTVFA THSTHKLLNA LSQASYIHVR
410 420 430 440 450
EGRGAINFSR FNQAYMMHAT TSPLYAICAS NDVAVSMMDG NSGLSLTQEV
460 470 480 490 500
IDEAVDFRQA MARLYKEFTA DGSWFFKPWN KEVVTDPQTG KTYDFADAPT
510 520 530 540 550
KLLTTVQDCW VMHPGESWHG FKDIPDNWSM LDPIKVSILA PGMGEDGELE
560 570 580 590 600
ETGVPAALVT AWLGRHGIVP TRTTDFQIMF LFSMGVTRGK WGTLVNTLCS
610 620 630 640 650
FKRHYDANTP LAQVMPELVE QYPDTYANMG IHDLGDTMFA WLKENNPGAR
660 670 680 690 700
LNEAYSGLPV AEVTPREAYN AIVDNNVELV SIENLPGRIA ANSVIPYPPG
710 720 730 740 750
IPMLLSGENF GDKNSPQVSY LRSLQSWDHH FPGFEHETEG TEIIDGIYHV

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751L → P(PubMed:2830169)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
SMRi P28629. Positions 1-755.
ModBasei Search...
MobiDBi 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.
InParanoidi P28629.
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: November 26, 2014
This is version 136 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