MEGL_FUSNN
ID MEGL_FUSNN Reviewed; 395 AA.
AC Q8RDT4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000303|PubMed:21798982};
DE Short=MGL {ECO:0000305};
DE EC=4.4.1.11 {ECO:0000250|UniProtKB:Q8L0X4};
DE AltName: Full=Homocysteine desulfhydrase {ECO:0000250|UniProtKB:Q8L0X4};
DE EC=4.4.1.2 {ECO:0000250|UniProtKB:Q8L0X4};
DE AltName: Full=L-cysteine desulfidase {ECO:0000305|PubMed:21798982};
DE EC=4.4.1.28 {ECO:0000269|PubMed:21798982};
GN OrderedLocusNames=FN1419 {ECO:0000312|EMBL:AAL95612.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=21798982; DOI=10.1099/mic.0.051813-0;
RA Suwabe K., Yoshida Y., Nagano K., Yoshimura F.;
RT "Identification of an L-methionine gamma-lyase involved in the production
RT of hydrogen sulfide from L-cysteine in Fusobacterium nucleatum subsp.
RT nucleatum ATCC 25586.";
RL Microbiology 157:2992-3000(2011).
CC -!- FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to
CC produce methanethiol, 2-oxobutanoate and ammonia, and that of L-
CC homocysteine (By similarity). Can also use L-cysteine as substrate,
CC catalyzing its alpha,beta-elimination; this activity seems to only
CC minimally contribute to the production of hydrogen sulfide (H2S) by
CC F.nucleatum in the oral cavity, which is toxic for a large variety of
CC cells in periodontal regions (PubMed:21798982).
CC {ECO:0000250|UniProtKB:Q8L0X4, ECO:0000269|PubMed:21798982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+);
CC Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11;
CC Evidence={ECO:0000250|UniProtKB:Q8L0X4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen
CC sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q8L0X4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35235; EC=4.4.1.28;
CC Evidence={ECO:0000269|PubMed:21798982};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P13254, ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for L-cysteine {ECO:0000269|PubMed:21798982};
CC Note=kcat is 0.69 sec(-1) for the production of H(2)S from L-
CC cysteine. {ECO:0000269|PubMed:21798982};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21798982}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC methionine gamma-lyase subfamily. {ECO:0000305}.
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DR EMBL; AE009951; AAL95612.1; -; Genomic_DNA.
DR RefSeq; NP_604313.1; NC_003454.1.
DR PDB; 6LXU; X-ray; 1.19 A; A=1-395.
DR PDB; 7BQW; X-ray; 2.50 A; A/B/C/D=1-395.
DR PDBsum; 6LXU; -.
DR PDBsum; 7BQW; -.
DR AlphaFoldDB; Q8RDT4; -.
DR SMR; Q8RDT4; -.
DR STRING; 190304.FN1419; -.
DR PRIDE; Q8RDT4; -.
DR EnsemblBacteria; AAL95612; AAL95612; FN1419.
DR KEGG; fnu:FN1419; -.
DR PATRIC; fig|190304.8.peg.1980; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR InParanoid; Q8RDT4; -.
DR OMA; THGGIIV; -.
DR BioCyc; FNUC190304:G1FZS-1989-MON; -.
DR BRENDA; 4.4.1.11; 11865.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0047982; F:homocysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:RHEA.
DR GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006237; L-Met_gamma_lys.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01328; met_gam_lyase; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..395
FT /note="L-methionine gamma-lyase"
FT /id="PRO_0000436012"
FT BINDING 56..58
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 86..87
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 206..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:7BQW"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:7BQW"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6LXU"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:6LXU"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6LXU"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6LXU"
FT TURN 207..212
FT /evidence="ECO:0007829|PDB:7BQW"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 260..279
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6LXU"
FT TURN 349..356
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:6LXU"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:6LXU"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:6LXU"
SQ SEQUENCE 395 AA; 43306 MW; 03C5C718EE3BA6DC CRC64;
MEMKKSGLGT TAIHAGTLKN LYGTLAMPIY QTSTFIFDSA EQGGRRFALE EAGYIYTRLG
NPTTTVLENK IAALEEGEAG IAMSSGMGAI SSTLWTVLKA GDHVVTDKTL YGCTFALMNH
GLTRFGVEVT FVDTSNLEEV KNAMKKNTRV VYLETPANPN LKIVDLEALS KIAHTNPNTL
VIVDNTFATP YMQKPLKLGV DIVVHSATKY LNGHGDVIAG LVVTRQELAD QIRFVGLKDM
TGAVLGPQEA YYIIRGLKTF EIRMERHCKN ARTIVDFLNK HPKVEKVYYP GLETHPGYEI
AKKQMKDFGA MISFELKGGF EAGKTLLNNL KLCSLAVSLG DTETLIQHPA SMTHSPYTKE
EREVAGITDG LVRLSVGLEN VEDIIADLEQ GLEKI
