UniProtKB - Q30W70 (CUTC_DESAG)
Protein
Choline trimethylamine-lyase
Gene
cutC
Organism
Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20))
Status
Functioni
Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde (PubMed:23151509, PubMed:24854437). Is involved in the anaerobic choline utilization pathway that allows D.alaskensis to grow on choline as a source of carbon and energy (PubMed:23151509). Is strictly specific for choline as substrate (PubMed:24854437).2 Publications
Catalytic activityi
- EC:4.3.99.4UniRule annotation1 Publication
Kineticsi
kcat is 747 sec(-1). Kinetic parameters measured with a CutC -52 AA truncated variant.1 Publication
- KM=302.5 µM for choline1 Publication
- Vmax=22.7 µmol/min/mg enzyme1 Publication
: choline degradation Pathwayi
This protein is involved in the pathway choline degradation, which is part of Amine and polyamine metabolism.UniRule annotation1 PublicationView all proteins of this organism that are known to be involved in the pathway choline degradation and in Amine and polyamine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 489 | Cysteine radical intermediateUniRule annotation2 Publications | 1 | |
Active sitei | 491 | Proton acceptorUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- carbon-nitrogen lyase activity Source: UniProtKB
- choline binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
GO - Biological processi
- choline catabolic process Source: UniProtKB
Keywordsi
Molecular function | Lyase |
Enzyme and pathway databases
BioCyci | DALA207559:G1G52-3076-MONOMER MetaCyc:MONOMER-17848 |
BRENDAi | 4.3.99.4, 1902 |
UniPathwayi | UPA01069 |
Names & Taxonomyi
Protein namesi | Recommended name: Choline trimethylamine-lyase1 PublicationUniRule annotation (EC:4.3.99.4UniRule annotation1 Publication)Short name: Choline TMA-lyase1 PublicationUniRule annotation Alternative name(s): Choline utilization protein C1 PublicationUniRule annotation Glycyl radical enzyme CutC1 Publication Short name: GRE CutC1 Publication |
Gene namesi | Name:cutC1 PublicationUniRule annotation Ordered Locus Names:Dde_3282Imported |
Organismi | Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans (strain G20)) |
Taxonomic identifieri | 207559 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene are unable to grow on choline, in contrast to wild-type, and do not produce TMA.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 216 | D → N: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 334 | T → S: About 2-fold decrease in catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 395 | F → L: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 489 | C → A: Loss of catalytic activity. Still activated by CutD but the remaining alpha-proton of the glycyl radical is no longer exchangeable. 2 Publications | 1 | |
Mutagenesisi | 491 | E → Q: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 502 | T → S: About 3-fold decrease in catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 821 | G → A: Loss of catalytic activity. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000435665 | 1 – 846 | Choline trimethylamine-lyaseAdd BLAST | 846 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 821 | Glycine radicalUniRule annotation2 Publications | 1 |
Post-translational modificationi
Requires the activating protein CutD to generate the key active site glycyl radical on Gly-821 that is involved in catalysis.UniRule annotation1 Publication
Keywords - PTMi
Organic radicalInteractioni
Subunit structurei
Homodimer.
1 PublicationGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 207559.Dde_3282 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q30W70 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 60 – 718 | PFLPROSITE-ProRule annotationAdd BLAST | 659 | |
Domaini | 725 – 846 | Glycine radicalPROSITE-ProRule annotationAdd BLAST | 122 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1882, Bacteria |
HOGENOMi | CLU_009096_0_1_7 |
OMAi | YCCETAP |
OrthoDBi | 116406at2 |
Family and domain databases
HAMAPi | MF_02058, Choline_CutC, 1 hit |
InterProi | View protein in InterPro IPR030897, Choline_CutC IPR019777, Form_AcTrfase_GR_CS IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
TIGRFAMsi | TIGR04394, choline_CutC, 1 hit |
PROSITEi | View protein in PROSITE PS00850, GLY_RADICAL_1, 1 hit PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
i Sequence
Sequence statusi: Complete.
Q30W70-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDLQDFSHKL AEATKNLTPA ERASLKKIFE GVSAEVFSQP APVSAVATGA
60 70 80 90 100
ESGIPDGPTP RHVKLKENFL KQVPSITVQR AVAITKIAKE NPGLPKPLLR
110 120 130 140 150
AKTFRYCCET APLVIQDHEL IVGSPNGAPR AGAFSPEVAW RWLQDELDTI
160 170 180 190 200
GSRPQDPFYI SEEDKKVLRE EVFPFWQNKS VDEFCEGQYR EADLWEMSGE
210 220 230 240 250
SFVSDCSYHA VNGGGDSNPG YDVILMKKGM LDIQREAREK LEQLDYANPE
260 270 280 290 300
DIDKIYFYKS VIETAEGVMI YARRLSAYAA ELAARETDPR RKAELQKISE
310 320 330 340 350
VNARVPAHAP SNFWEAIQAV WTVESLLVVE ENQTGMSIGR VDQYMYPFYR
360 370 380 390 400
ADIDSGRLTE YEAFDLAGCM LVKMSEMMWI TSEGASKFFA GYQPFVNMCV
410 420 430 440 450
GGVTREGHDA TNDLTYMLMD AVRHVRIYQP TLATRVHNKS PQKYLKKIVD
460 470 480 490 500
VIRSGMGFPA VHFDDAHIKM MLAKGVSIED ARDYCLMGCV EPQKSGRLYQ
510 520 530 540 550
WTSTGYTQWP ICIELVLNHG VPLWYGKKVT PDMGDLSQYD TYEKFEAAVK
560 570 580 590 600
EQIRWITKNT SVATVISQRA HRELAPKPLM SLMYEGCMES GRDVSAGGAM
610 620 630 640 650
YNFGPGVVWS GLATYVDSMA AIKKLVYDDR KYTLAQLNEA LKADFAGYDQ
660 670 680 690 700
ILADCLAAPK YGNDDDYADM IAADLVHFTE TEHRKYKTLY SVLSHGTLSI
710 720 730 740 750
SNNTPFGQLL GASANGRRAW MPLSDGISPT QGADYKGPTA IIKSVSKMAN
760 770 780 790 800
DNMNIGMVHN FKLMSGLLDT PEGENGLITL IRTACMLGNG EMQFNYLDNE
810 820 830 840
LLLDAQKHPE KYRDLVVRVA GYSAFFVELC KDVQDEIISR TMLHGF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000112 Genomic DNA Translation: ABB40076.1 |
RefSeqi | WP_011369019.1, NC_007519.1 |
Genome annotation databases
EnsemblBacteriai | ABB40076; ABB40076; Dde_3282 |
KEGGi | dde:Dde_3282 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000112 Genomic DNA Translation: ABB40076.1 |
RefSeqi | WP_011369019.1, NC_007519.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5FAU | X-ray | 1.90 | A/B/C/D | 19-846 | [»] | |
5FAV | X-ray | 1.60 | A/B | 53-846 | [»] | |
5FAW | X-ray | 1.85 | A/B | 53-846 | [»] | |
5FAY | X-ray | 1.90 | A/B | 53-846 | [»] | |
5KDP | X-ray | 1.90 | A/C | 53-846 | [»] | |
6ND3 | X-ray | 2.36 | A/B/C/D/E/F/G/H | 19-846 | [»] | |
SMRi | Q30W70 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 207559.Dde_3282 |
Genome annotation databases
EnsemblBacteriai | ABB40076; ABB40076; Dde_3282 |
KEGGi | dde:Dde_3282 |
Phylogenomic databases
eggNOGi | COG1882, Bacteria |
HOGENOMi | CLU_009096_0_1_7 |
OMAi | YCCETAP |
OrthoDBi | 116406at2 |
Enzyme and pathway databases
UniPathwayi | UPA01069 |
BioCyci | DALA207559:G1G52-3076-MONOMER MetaCyc:MONOMER-17848 |
BRENDAi | 4.3.99.4, 1902 |
Family and domain databases
HAMAPi | MF_02058, Choline_CutC, 1 hit |
InterProi | View protein in InterPro IPR030897, Choline_CutC IPR019777, Form_AcTrfase_GR_CS IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
TIGRFAMsi | TIGR04394, choline_CutC, 1 hit |
PROSITEi | View protein in PROSITE PS00850, GLY_RADICAL_1, 1 hit PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CUTC_DESAG | |
Accessioni | Q30W70Primary (citable) accession number: Q30W70 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 16, 2016 |
Last sequence update: | December 6, 2005 | |
Last modified: | December 2, 2020 | |
This is version 83 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families