MTAD_THEMA
ID MTAD_THEMA Reviewed; 406 AA.
AC Q9X034;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase;
DE Short=MTA/SAH deaminase;
DE EC=3.5.4.28;
DE EC=3.5.4.31;
GN Name=mtaD; OrderedLocusNames=TM_0936;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-5, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX
RP WITH ZINC ION AND PRODUCT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=17603473; DOI=10.1038/nature05981;
RA Hermann J.C., Marti-Arbona R., Fedorov A.A., Fedorov E., Almo S.C.,
RA Shoichet B.K., Raushel F.M.;
RT "Structure-based activity prediction for an enzyme of unknown function.";
RL Nature 448:775-779(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NICKEL ION AND
RP METHIONINE.
RG New York structural genomics research consortium (NYSGRC);
RT "Structure of the hypothetical protein TM0936 from Thermotoga maritima at
RT 1.5 A bound to Ni and methionine.";
RL Submitted (JAN-2005) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NICKEL ION.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of metal-dependent hydrolase of
RT cytosinedemaniase/chlorohydrolase family (TM0936) from Thermotoga maritima
RT at 1.9 A resolution.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and S-
CC adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-
CC homocysteine, respectively. Is also able to deaminate adenosine.
CC Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are
CC not enzyme substrates. {ECO:0000269|PubMed:17603473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-
CC homocysteine; Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57985; EC=3.5.4.28;
CC Evidence={ECO:0000269|PubMed:17603473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-
CC thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:48595; EC=3.5.4.31;
CC Evidence={ECO:0000269|PubMed:17603473};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17603473};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17603473};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for S-adenosyl-L-homocysteine
CC {ECO:0000269|PubMed:17603473};
CC KM=44 uM for 5-methyl-thioadenosine {ECO:0000269|PubMed:17603473};
CC KM=250 uM for adenosine {ECO:0000269|PubMed:17603473};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC MTA/SAH deaminase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36017.1; -; Genomic_DNA.
DR PIR; H72315; H72315.
DR RefSeq; NP_228744.1; NC_000853.1.
DR RefSeq; WP_004080626.1; NZ_CP011107.1.
DR PDB; 1J6P; X-ray; 1.90 A; A=1-406.
DR PDB; 1P1M; X-ray; 1.50 A; A=1-406.
DR PDB; 2PLM; X-ray; 2.10 A; A=1-406.
DR PDBsum; 1J6P; -.
DR PDBsum; 1P1M; -.
DR PDBsum; 2PLM; -.
DR AlphaFoldDB; Q9X034; -.
DR SMR; Q9X034; -.
DR STRING; 243274.THEMA_09670; -.
DR ChEMBL; CHEMBL1075031; -.
DR PRIDE; Q9X034; -.
DR EnsemblBacteria; AAD36017; AAD36017; TM_0936.
DR KEGG; tma:TM0936; -.
DR eggNOG; COG0402; Bacteria.
DR InParanoid; Q9X034; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 1592010at2; -.
DR BioCyc; MetaCyc:MON-16147; -.
DR BRENDA; 3.5.4.31; 6331.
DR SABIO-RK; Q9X034; -.
DR EvolutionaryTrace; Q9X034; -.
DR PRO; PR:Q9X034; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IDA:CACAO.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_01281; MTA_SAH_deamin; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR023512; Deaminase_MtaD/DadD.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..406
FT /note="5-methylthioadenosine/S-adenosylhomocysteine
FT deaminase"
FT /id="PRO_0000312465"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 84
FT /ligand="substrate"
FT BINDING 136
FT /ligand="substrate"
FT BINDING 148
FT /ligand="substrate"
FT BINDING 173
FT /ligand="substrate"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 203
FT /ligand="substrate"
FT BINDING 279
FT /ligand="substrate"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:1P1M"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:1P1M"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1P1M"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1P1M"
FT TURN 237..242
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1P1M"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1P1M"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:1P1M"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:1P1M"
SQ SEQUENCE 406 AA; 45773 MW; 3437565703ECC544 CRC64;
MIIGNCLILK DFSSEPFWGA VEIENGTIKR VLQGEVKVDL DLSGKLVMPA LFNTHTHAPM
TLLRGVAEDL SFEEWLFSKV LPIEDRLTEK MAYYGTILAQ MEMARHGIAG FVDMYFHEEW
IAKAVRDFGM RALLTRGLVD SNGDDGGRLE ENLKLYNEWN GFEGRIFVGF GPHSPYLCSE
EYLKRVFDTA KSLNAPVTIH LYETSKEEYD LEDILNIGLK EVKTIAAHCV HLPERYFGVL
KDIPFFVSHN PASNLKLGNG IAPVQRMIEH GMKVTLGTDG AASNNSLNLF FEMRLASLLQ
KAQNPRNLDV NTCLKMVTYD GAQAMGFKSG KIEEGWNADL VVIDLDLPEM FPVQNIKNHL
VHAFSGEVFA TMVAGKWIYF DGEYPTIDSE EVKRELARIE KELYSS
