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P43099

- DCOR_LACS3

UniProt

P43099 - DCOR_LACS3

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Protein

Ornithine decarboxylase, inducible

Gene

odcI

Organism
Lactobacillus sp. (strain 30a)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. ornithine decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

SABIO-RKP43099.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase, inducible (EC:4.1.1.17)
Short name:
ODC
Gene namesi
Name:odcI
OrganismiLactobacillus sp. (strain 30a)
Taxonomic identifieri1593 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 731730Ornithine decarboxylase, induciblePRO_0000201137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei356 – 3561N6-(pyridoxal phosphate)lysine

Expressioni

Inductioni

By ornithine.

Interactioni

Subunit structurei

Dodecamer.

Structurei

Secondary structure

1
731
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94
Helixi11 – 166
Beta strandi27 – 293
Beta strandi31 – 4010
Helixi44 – 518
Beta strandi59 – 646
Helixi66 – 683
Helixi71 – 744
Beta strandi79 – 824
Helixi92 – 10716
Helixi110 – 11910
Beta strandi127 – 1293
Turni130 – 1367
Helixi137 – 1393
Helixi141 – 15010
Helixi153 – 1564
Helixi164 – 1663
Turni169 – 1724
Helixi175 – 18612
Beta strandi190 – 1978
Helixi198 – 21013
Beta strandi216 – 2205
Helixi225 – 2317
Turni232 – 2354
Beta strandi238 – 2425
Beta strandi244 – 2463
Beta strandi252 – 2554
Helixi257 – 2593
Helixi262 – 2687
Turni269 – 2713
Helixi274 – 2774
Beta strandi283 – 2919
Beta strandi295 – 2984
Helixi300 – 3078
Helixi308 – 3103
Beta strandi311 – 3177
Helixi323 – 3253
Helixi328 – 3336
Beta strandi347 – 3526
Helixi354 – 3574
Beta strandi365 – 3706
Helixi372 – 3743
Beta strandi375 – 3795
Helixi383 – 39311
Helixi400 – 41314
Helixi415 – 43824
Beta strandi442 – 4476
Beta strandi449 – 4513
Helixi456 – 4583
Helixi461 – 4644
Helixi468 – 4714
Turni478 – 4803
Beta strandi490 – 4923
Beta strandi496 – 5005
Beta strandi502 – 5054
Turni506 – 5094
Helixi518 – 52710
Beta strandi533 – 5353
Beta strandi537 – 5437
Helixi550 – 56819
Helixi573 – 5764
Helixi578 – 5814
Turni585 – 5873
Helixi593 – 60513
Turni606 – 6083
Helixi609 – 6157
Helixi619 – 6213
Beta strandi624 – 6274
Helixi629 – 6379
Beta strandi641 – 6455
Turni646 – 6483
Beta strandi652 – 6565
Beta strandi658 – 6603
Turni661 – 6633
Helixi676 – 69116
Beta strandi699 – 7079
Beta strandi710 – 7189
Helixi720 – 7245
Helixi727 – 7293

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4KX-ray2.70A2-731[»]
1ORDX-ray3.00A/B2-731[»]
ProteinModelPortaliP43099.
SMRiP43099. Positions 2-731.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43099.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.220. 1 hit.
3.40.640.10. 1 hit.
3.90.100.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR005308. OKR_de-COase_N.
IPR011193. Orn/lys/arg_de-COase.
IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
IPR027464. Ornithine_deCO2ase_N.
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.
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF53383. SSF53383. 1 hit.
SSF55904. SSF55904. 1 hit.
PROSITEiPS00703. OKR_DC_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43099-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSLKIAST QEARQYFDTD RVVVDAVGSD FTDVGAVIAM DYETDVIDAA
60 70 80 90 100
DATKFGIPVF AVTKDAQAIS ADELKKIFHI IDLENKFDAT VNAREIETAV
110 120 130 140 150
NNYEDSILPP FFKSLKEYVS RGLIQFDCPG HQGGQYYRKH PAGREFYDFF
160 170 180 190 200
GETVFRADLC NADVALGDLL IHEGPAVAAE KHAARVYNAD KTYFVLGGSS
210 220 230 240 250
NANNTVTSAL VSNGDLVLFD RNNHKSVYNS ALAMAGGRPV YLQTNRNPYG
260 270 280 290 300
FIGGIYDSDF DEKKIRELAA KVDPERAKWK RPFRLAVIQL GTYDGTIYNA
310 320 330 340 350
HEVVKRIGHL CDYIEFDSAW VGYEQFIPMM RNSSPLLIDD LGPEDPGIIV
360 370 380 390 400
VQSVHKQQAG FSQTSQIHKK DSHIKGQLRY CDHKHFNNSF NLFMSTSPFY
410 420 430 440 450
PMYAALDVNA AMQEGEAGRK LWHDLLITTI EARKKLIKAG SMFRPFVPPV
460 470 480 490 500
VNGKKWEDGD TEDMANNIDY WRFEKGAKWH AYEGYGDNQY YVDPNKFMLT
510 520 530 540 550
TPGINPETGD YEDFGVPATI VANYLRDHGI IPEKSDLNSI LFLMTPAETP
560 570 580 590 600
AKMNNLITQL LQLQRLIEED APLKQVLPSI YAANEERYNG YTIRELCQEL
610 620 630 640 650
HDFYKNNNTF TYQKRLFLRE FFPEQGMLPY EARQEFIRNH NKLVPLNKIE
660 670 680 690 700
GEIALEGALP YPPGVFCVAP GEKWSETAVK YFTILQDGIN NFPGFAPEIQ
710 720 730
GVYFKQEGDK VVAYGEVYDA EVAKNDDRYN N
Length:731
Mass (Da):82,688
Last modified:January 23, 2007 - v2
Checksum:i3652214455C956AF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11816 Genomic DNA. Translation: AAA64830.1.
PIRiA55229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11816 Genomic DNA. Translation: AAA64830.1 .
PIRi A55229.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C4K X-ray 2.70 A 2-731 [» ]
1ORD X-ray 3.00 A/B 2-731 [» ]
ProteinModelPortali P43099.
SMRi P43099. Positions 2-731.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P43099.

Miscellaneous databases

EvolutionaryTracei P43099.

Family and domain databases

Gene3Di 3.40.50.220. 1 hit.
3.40.640.10. 1 hit.
3.90.100.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR011006. CheY-like_superfamily.
IPR005308. OKR_de-COase_N.
IPR011193. Orn/lys/arg_de-COase.
IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
IPR027464. Ornithine_deCO2ase_N.
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 SSF52172. SSF52172. 1 hit.
SSF53383. SSF53383. 1 hit.
SSF55904. SSF55904. 1 hit.
PROSITEi PS00703. OKR_DC_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence of ornithine decarboxylase from Lactobacillus sp. strain 30a."
    Hackert M.L., Carroll D.W., Davidson L., Kim S.-O., Momany C., Vaaler G.L., Zhang L.
    J. Bacteriol. 176:7391-7394(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0-A resolution."
    Momany C., Ernst S., Gosh R., Chang N.-L., Hackert M.L.
    J. Mol. Biol. 252:643-655(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  3. "Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a."
    Vitali J., Carroll D., Chaudhry R.G., Hackert M.L.
    Acta Crystallogr. D 55:1978-1985(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  4. "Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase."
    Momany C., Gosh R., Hackert M.L.
    Protein Sci. 4:849-854(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.

Entry informationi

Entry nameiDCOR_LACS3
AccessioniPrimary (citable) accession number: P43099
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 83 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3