GENTAUR Molecular Products.

 CUTC_DESAG              Reviewed;         846 AA.
 Q30W70;
 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
 06-DEC-2005, sequence version 1.
 28-FEB-2018, entry version 75.
 RecName: Full=Choline trimethylamine-lyase {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000303|PubMed:23151509};
          Short=Choline TMA-lyase {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000303|PubMed:23151509};
          EC=4.3.99.4 {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000269|PubMed:23151509};
 AltName: Full=Choline utilization protein C {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000303|PubMed:23151509};
 AltName: Full=Glycyl radical enzyme CutC {ECO:0000303|PubMed:23151509};
          Short=GRE CutC {ECO:0000303|PubMed:24854437};
 Name=cutC {ECO:0000255|HAMAP-Rule:MF_02058,
 ECO:0000303|PubMed:23151509};
 OrderedLocusNames=Dde_3282 {ECO:0000312|EMBL:ABB40076.1};
 Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans
 (strain G20)).
 Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
 Desulfovibrionaceae; Desulfovibrio.
 NCBI_TaxID=207559;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=G20;
 PubMed=21685289; DOI=10.1128/JB.05400-11;
 Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
 Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C.,
 Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A.,
 Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
 "Complete genome sequence and updated annotation of Desulfovibrio
 alaskensis G20.";
 J. Bacteriol. 193:4268-4269(2011).
 [2]
 IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE,
 GLYCYL RADICAL AT GLY-821, PATHWAY, AND MUTAGENESIS OF CYS-489 AND
 GLY-821.
 STRAIN=G20;
 PubMed=23151509; DOI=10.1073/pnas.1215689109;
 Craciun S., Balskus E.P.;
 "Microbial conversion of choline to trimethylamine requires a glycyl
 radical enzyme.";
 Proc. Natl. Acad. Sci. U.S.A. 109:21307-21312(2012).
 [3]
 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
 SPECIFICITY, SUBUNIT, MUTAGENESIS OF ASP-216; THR-334; PHE-395;
 CYS-489; GLU-491; THR-502 AND GLY-821, REACTION MECHANISM, AND
 3D-STRUCTURE MODELING.
 STRAIN=G20;
 PubMed=24854437; DOI=10.1021/cb500113p;
 Craciun S., Marks J.A., Balskus E.P.;
 "Characterization of choline trimethylamine-lyase expands the
 chemistry of glycyl radical enzymes.";
 ACS Chem. Biol. 9:1408-1413(2014).
 -!- FUNCTION: 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). {ECO:0000269|PubMed:23151509,
     ECO:0000269|PubMed:24854437}.
 -!- CATALYTIC ACTIVITY: Choline = trimethylamine + acetaldehyde.
     {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000269|PubMed:23151509}.
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=302.5 uM for choline {ECO:0000269|PubMed:24854437};
       Vmax=22.7 umol/min/mg enzyme {ECO:0000269|PubMed:24854437};
       Note=kcat is 747 sec(-1). Kinetic parameters measured with a
       CutC -52 AA truncated variant. {ECO:0000269|PubMed:24854437};
 -!- PATHWAY: Amine and polyamine metabolism; choline degradation.
     {ECO:0000255|HAMAP-Rule:MF_02058, ECO:0000269|PubMed:23151509}.
 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24854437}.
 -!- PTM: Requires the activating protein CutD to generate the key
     active site glycyl radical on Gly-821 that is involved in
     catalysis. {ECO:0000255|HAMAP-Rule:MF_02058,
     ECO:0000269|PubMed:23151509}.
 -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
     on choline, in contrast to wild-type, and do not produce TMA.
     {ECO:0000269|PubMed:23151509}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; CP000112; ABB40076.1; -; Genomic_DNA.
 RefSeq; WP_011369019.1; NC_007519.1.
 PDB; 5FAU; X-ray; 1.90 A; A/B/C/D=19-846.
 PDB; 5FAV; X-ray; 1.60 A; A/B=53-846.
 PDB; 5FAW; X-ray; 1.85 A; A/B=53-846.
 PDB; 5FAY; X-ray; 1.90 A; A/B=53-846.
 PDB; 5KDP; X-ray; 1.90 A; A/C=53-846.
 PDBsum; 5FAU; -.
 PDBsum; 5FAV; -.
 PDBsum; 5FAW; -.
 PDBsum; 5FAY; -.
 PDBsum; 5KDP; -.
 SMR; Q30W70; -.
 STRING; 207559.Dde_3282; -.
 EnsemblBacteria; ABB40076; ABB40076; Dde_3282.
 KEGG; dde:Dde_3282; -.
 eggNOG; ENOG4105C6N; Bacteria.
 eggNOG; COG1882; LUCA.
 HOGENOM; HOG000274401; -.
 KO; K20038; -.
 OMA; YCCETAP; -.
 OrthoDB; POG091H0HBJ; -.
 BioCyc; DALA207559:G1G52-3076-MONOMER; -.
 BioCyc; MetaCyc:MONOMER-17848; -.
 BRENDA; 4.3.99.4; 1902.
 UniPathway; UPA01069; -.
 Proteomes; UP000002710; Chromosome.
 GO; GO:0016840; F:carbon-nitrogen lyase activity; IDA:UniProtKB.
 GO; GO:0033265; F:choline binding; IDA:UniProtKB.
 GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO; GO:0042426; P:choline catabolic process; IDA:UniProtKB.
 HAMAP; MF_02058; Choline_CutC; 1.
 InterPro; IPR030897; Choline_CutC.
 InterPro; IPR019777; Form_AcTrfase_GR_CS.
 InterPro; IPR001150; Gly_radical.
 InterPro; IPR004184; PFL_dom.
 Pfam; PF01228; Gly_radical; 1.
 Pfam; PF02901; PFL-like; 1.
 TIGRFAMs; TIGR04394; choline_CutC; 1.
 PROSITE; PS00850; GLY_RADICAL_1; 1.
 PROSITE; PS51149; GLY_RADICAL_2; 1.
 PROSITE; PS51554; PFL; 1.
 1: Evidence at protein level;
 3D-structure; Complete proteome; Lyase; Organic radical;
 Reference proteome.
 CHAIN         1    846       Choline trimethylamine-lyase.
                              /FTId=PRO_0000435665.
 DOMAIN       60    718       PFL. {ECO:0000255|PROSITE-
                              ProRule:PRU00887}.
 DOMAIN      725    846       Glycine radical. {ECO:0000255|PROSITE-
                              ProRule:PRU00493}.
 ACT_SITE    489    489       Cysteine radical intermediate.
                              {ECO:0000255|HAMAP-Rule:MF_02058,
                              ECO:0000305|PubMed:23151509,
                              ECO:0000305|PubMed:24854437}.
 ACT_SITE    491    491       Proton acceptor. {ECO:0000255|HAMAP-
                              Rule:MF_02058,
                              ECO:0000305|PubMed:24854437}.
 MOD_RES     821    821       Glycine radical. {ECO:0000255|HAMAP-
                              Rule:MF_02058,
                              ECO:0000305|PubMed:23151509,
                              ECO:0000305|PubMed:24854437}.
 MUTAGEN     216    216       D->N: Loss of catalytic activity.
                              {ECO:0000269|PubMed:24854437}.
 MUTAGEN     334    334       T->S: About 2-fold decrease in catalytic
                              activity. {ECO:0000269|PubMed:24854437}.
 MUTAGEN     395    395       F->L: Loss of catalytic activity.
                              {ECO:0000269|PubMed:24854437}.
 MUTAGEN     489    489       C->A: Loss of catalytic activity. Still
                              activated by CutD but the remaining
                              alpha-proton of the glycyl radical is no
                              longer exchangeable.
                              {ECO:0000269|PubMed:23151509,
                              ECO:0000269|PubMed:24854437}.
 MUTAGEN     491    491       E->Q: Loss of catalytic activity.
                              {ECO:0000269|PubMed:24854437}.
 MUTAGEN     502    502       T->S: About 3-fold decrease in catalytic
                              activity. {ECO:0000269|PubMed:24854437}.
 MUTAGEN     821    821       G->A: Loss of catalytic activity.
                              {ECO:0000269|PubMed:23151509,
                              ECO:0000269|PubMed:24854437}.
 HELIX        60     70       {ECO:0000244|PDB:5FAV}.
 STRAND       75     77       {ECO:0000244|PDB:5FAV}.
 HELIX        79     90       {ECO:0000244|PDB:5FAV}.
 HELIX        96    110       {ECO:0000244|PDB:5FAV}.
 STRAND      131    133       {ECO:0000244|PDB:5FAV}.
 TURN        136    138       {ECO:0000244|PDB:5FAV}.
 HELIX       141    146       {ECO:0000244|PDB:5FAV}.
 TURN        147    152       {ECO:0000244|PDB:5FAV}.
 STRAND      154    156       {ECO:0000244|PDB:5FAV}.
 HELIX       162    170       {ECO:0000244|PDB:5FAV}.
 HELIX       172    176       {ECO:0000244|PDB:5FAV}.
 TURN        177    179       {ECO:0000244|PDB:5FAV}.
 HELIX       181    191       {ECO:0000244|PDB:5FAV}.
 HELIX       195    198       {ECO:0000244|PDB:5FAV}.
 STRAND      203    205       {ECO:0000244|PDB:5FAV}.
 HELIX       208    211       {ECO:0000244|PDB:5FAV}.
 HELIX       221    225       {ECO:0000244|PDB:5FAV}.
 HELIX       230    242       {ECO:0000244|PDB:5FAV}.
 HELIX       249    251       {ECO:0000244|PDB:5FAV}.
 HELIX       252    285       {ECO:0000244|PDB:5FAV}.
 HELIX       289    304       {ECO:0000244|PDB:5FAV}.
 TURN        305    307       {ECO:0000244|PDB:5FAV}.
 HELIX       313    330       {ECO:0000244|PDB:5FAV}.
 HELIX       341    344       {ECO:0000244|PDB:5FAV}.
 HELIX       346    355       {ECO:0000244|PDB:5FAV}.
 STRAND      356    358       {ECO:0000244|PDB:5FAV}.
 HELIX       360    375       {ECO:0000244|PDB:5FAV}.
 HELIX       383    386       {ECO:0000244|PDB:5FAV}.
 HELIX       387    389       {ECO:0000244|PDB:5FAV}.
 TURN        390    392       {ECO:0000244|PDB:5FAV}.
 STRAND      397    403       {ECO:0000244|PDB:5FAV}.
 STRAND      407    409       {ECO:0000244|PDB:5FAV}.
 HELIX       413    425       {ECO:0000244|PDB:5FAV}.
 STRAND      430    436       {ECO:0000244|PDB:5FAV}.
 HELIX       442    453       {ECO:0000244|PDB:5FAV}.
 STRAND      460    463       {ECO:0000244|PDB:5FAV}.
 HELIX       464    473       {ECO:0000244|PDB:5FAV}.
 HELIX       478    482       {ECO:0000244|PDB:5FAV}.
 STRAND      485    487       {ECO:0000244|PDB:5FAV}.
 TURN        488    490       {ECO:0000244|PDB:5FAV}.
 STRAND      491    493       {ECO:0000244|PDB:5FAV}.
 TURN        495    497       {ECO:0000244|PDB:5FAV}.
 STRAND      503    509       {ECO:0000244|PDB:5FAV}.
 HELIX       510    517       {ECO:0000244|PDB:5FAV}.
 TURN        518    520       {ECO:0000244|PDB:5FAV}.
 TURN        523    525       {ECO:0000244|PDB:5FAV}.
 HELIX       536    538       {ECO:0000244|PDB:5FAV}.
 HELIX       542    574       {ECO:0000244|PDB:5FAV}.
 HELIX       578    582       {ECO:0000244|PDB:5FAV}.
 HELIX       587    590       {ECO:0000244|PDB:5FAV}.
 HELIX       594    596       {ECO:0000244|PDB:5FAV}.
 STRAND      599    602       {ECO:0000244|PDB:5FAV}.
 STRAND      606    610       {ECO:0000244|PDB:5FAV}.
 HELIX       612    626       {ECO:0000244|PDB:5FAV}.
 HELIX       634    642       {ECO:0000244|PDB:5FAV}.
 TURN        643    647       {ECO:0000244|PDB:5FAV}.
 HELIX       649    657       {ECO:0000244|PDB:5FAV}.
 HELIX       666    683       {ECO:0000244|PDB:5FAV}.
 STRAND      689    692       {ECO:0000244|PDB:5FAV}.
 STRAND      694    697       {ECO:0000244|PDB:5FAV}.
 TURN        700    702       {ECO:0000244|PDB:5FAV}.
 HELIX       703    708       {ECO:0000244|PDB:5FAV}.
 TURN        731    733       {ECO:0000244|PDB:5FAV}.
 HELIX       738    746       {ECO:0000244|PDB:5FAV}.
 HELIX       750    752       {ECO:0000244|PDB:5FAV}.
 STRAND      760    764       {ECO:0000244|PDB:5FAV}.
 HELIX       767    769       {ECO:0000244|PDB:5FAV}.
 HELIX       771    787       {ECO:0000244|PDB:5FAV}.
 STRAND      791    797       {ECO:0000244|PDB:5FAV}.
 HELIX       799    807       {ECO:0000244|PDB:5FAV}.
 HELIX       809    811       {ECO:0000244|PDB:5FAV}.
 STRAND      816    818       {ECO:0000244|PDB:5FAV}.
 STRAND      820    825       {ECO:0000244|PDB:5FAV}.
 HELIX       826    828       {ECO:0000244|PDB:5FAV}.
 HELIX       831    839       {ECO:0000244|PDB:5FAV}.
 SEQUENCE   846 AA;  94640 MW;  8CF56E2D011D7DDD CRC64;
 MDLQDFSHKL AEATKNLTPA ERASLKKIFE GVSAEVFSQP APVSAVATGA ESGIPDGPTP
 RHVKLKENFL KQVPSITVQR AVAITKIAKE NPGLPKPLLR AKTFRYCCET APLVIQDHEL
 IVGSPNGAPR AGAFSPEVAW RWLQDELDTI GSRPQDPFYI SEEDKKVLRE EVFPFWQNKS
 VDEFCEGQYR EADLWEMSGE SFVSDCSYHA VNGGGDSNPG YDVILMKKGM LDIQREAREK
 LEQLDYANPE DIDKIYFYKS VIETAEGVMI YARRLSAYAA ELAARETDPR RKAELQKISE
 VNARVPAHAP SNFWEAIQAV WTVESLLVVE ENQTGMSIGR VDQYMYPFYR ADIDSGRLTE
 YEAFDLAGCM LVKMSEMMWI TSEGASKFFA GYQPFVNMCV GGVTREGHDA TNDLTYMLMD
 AVRHVRIYQP TLATRVHNKS PQKYLKKIVD VIRSGMGFPA VHFDDAHIKM MLAKGVSIED
 ARDYCLMGCV EPQKSGRLYQ WTSTGYTQWP ICIELVLNHG VPLWYGKKVT PDMGDLSQYD
 TYEKFEAAVK EQIRWITKNT SVATVISQRA HRELAPKPLM SLMYEGCMES GRDVSAGGAM
 YNFGPGVVWS GLATYVDSMA AIKKLVYDDR KYTLAQLNEA LKADFAGYDQ ILADCLAAPK
 YGNDDDYADM IAADLVHFTE TEHRKYKTLY SVLSHGTLSI SNNTPFGQLL GASANGRRAW
 MPLSDGISPT QGADYKGPTA IIKSVSKMAN DNMNIGMVHN FKLMSGLLDT PEGENGLITL
 IRTACMLGNG EMQFNYLDNE LLLDAQKHPE KYRDLVVRVA GYSAFFVELC KDVQDEIISR
 TMLHGF

Related products :