ID E4RLP5_HALHG Unreviewed; 433 AA.
AC E4RLP5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE Short=MTA/SAH deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE EC=3.5.4.28 {ECO:0000256|HAMAP-Rule:MF_01281};
DE EC=3.5.4.31 {ECO:0000256|HAMAP-Rule:MF_01281};
GN Name=mtaD {ECO:0000256|HAMAP-Rule:MF_01281};
GN OrderedLocusNames=Halsa_1534 {ECO:0000313|EMBL:ADQ14959.1};
OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ14959.1, ECO:0000313|Proteomes:UP000007434};
RN [1] {ECO:0000313|EMBL:ADQ14959.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT "Complete sequence of Halanaerobium sp. sapolanicus.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ14959.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX PubMed=21602336; DOI=10.1128/JB.05209-11;
RA Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT Halanaerobium hydrogenoformans.";
RL J. Bacteriol. 193:3682-3683(2011).
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 {ECO:0000256|HAMAP-Rule:MF_01281}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01281};
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01281};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01281};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01281};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC MTA/SAH deaminase family. {ECO:0000256|HAMAP-Rule:MF_01281}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01281}.
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DR EMBL; CP002304; ADQ14959.1; -; Genomic_DNA.
DR RefSeq; WP_013406036.1; NC_014654.1.
DR AlphaFoldDB; E4RLP5; -.
DR STRING; 656519.Halsa_1534; -.
DR KEGG; has:Halsa_1534; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_1_9; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000007434; 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; IEA:UniProtKB-UniRule.
DR CDD; cd01298; ATZ_TRZ_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01281};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW Reference proteome {ECO:0000313|Proteomes:UP000007434};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT DOMAIN 57..403
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 433 AA; 47946 MW; 246A8794E1D5BCC1 CRC64;
MGILIKNILE IYSGVEPEPL KNQYLIIEDD KIKEISAMDS CPTKKDFSEV IDAEGKILLP
GLINTHTHTA MTLMRGYADD MPLQKWLQTK IWPFEAKLKG DDIYWGTALG VLEMLKGGTT
AFADMYFAMD RAAEVVDKSG IRAVLAEGLI EANDGDTGLK NSLDFALEYN NSAEGRITTM
LAPHAPYTCS RSYLEKITKL AADNNLAVHI HLSETKKEVN DFMSDHSLSP IKFLAEFDFF
KNHILAAHVV HPEPGDLEIL KKNRVNIAHN PISNAKLGSG IAPIADYLAA DINVSIGTDG
VSSNNNLDLI TEARMAAYLQ KVNNYDPSLI DTQQLLEMLT INGAKTLNLA QIGMIKEGKK
ADLILVDTQN NTFSYPHHNN LSNLFYAADS RIIDTVIING KIIVYGGEIK TLDQEKIYYQ
AEKSAKRIAD NLK
//
