ID A0A061QDS0_9PROT Unreviewed; 469 AA.
AC A0A061QDS0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000313|EMBL:GAK34315.1};
GN Name=mtaD {ECO:0000313|EMBL:GAK34315.1};
GN ORFNames=AQ1_02213 {ECO:0000313|EMBL:GAK34315.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK34315.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK34315.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK34315.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK34315.1}.
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DR EMBL; BAYV01000029; GAK34315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QDS0; -.
DR STRING; 1492281.AQ1_02213; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000027360; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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 InterPro; IPR006680; Amidohydro-rel.
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 Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001609813"
FT DOMAIN 78..432
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 469 AA; 51035 MW; B7935C174FBC0D35 CRC64;
MFRFVAALCV GLIGAPLAQA EKVDLLITNA TLVTMDGSRQ VIDQGVVAIR DRLIVKVGGP
ALAADYEPER LIDAGGDIVM PGMINLHNHI SMVAFRGLGE YEVENLLFDV MFPLEKELLN
RQLIRVSARQ SAIELAMGGV TSFADMYYHE DEVAIAVKDV GLRGVLGQTV IGFPVVDSPK
PYGGLAYAED FIRKYQGDEL ITPAIAPHAP YTVDKEQLLA AKAISDQYDV PMLMHLVEFP
NEYEMVLERH PDMANYRSEI SYLDQIGFLG PKLLAAHVLY LDDADMDLLK ARGVGVSHNP
KANSKGASGI SPAWEMMKKG LDIGLGTDGP MSSNQMDILT VMHYVASVAR LRLMDATPYT
PLELVEMATI GGAQALDRGD DLGSLEAGKL ADLIIIDRDA PNMQPGYDVY AAIAFGAYPG
NVETTIVNGQ VVMHDRMIET VDLAAHEAEW TEVKSRVEAF AKTLEGGIR
//