ID Q8TLS5_METAC Unreviewed; 530 AA.
AC Q8TLS5;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN OrderedLocusNames=MA_2953 {ECO:0000313|EMBL:AAM06327.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM06327.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM06327.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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DR EMBL; AE010299; AAM06327.1; -; Genomic_DNA.
DR RefSeq; WP_011022897.1; NC_003552.1.
DR AlphaFoldDB; Q8TLS5; -.
DR STRING; 188937.MA_2953; -.
DR DNASU; 1474847; -.
DR EnsemblBacteria; AAM06327; AAM06327; MA_2953.
DR GeneID; 1474847; -.
DR KEGG; mac:MA_2953; -.
DR HOGENOM; CLU_009942_6_1_2; -.
DR InParanoid; Q8TLS5; -.
DR OrthoDB; 8791at2157; -.
DR PhylomeDB; Q8TLS5; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 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; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT DOMAIN 56..527
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 530 AA; 57711 MW; 07810C7C61804FB9 CRC64;
MENTVDAKKD STIAFTGGRI LTMDSEQKYA EAVVIRGDRI AAVGGTYILK SFPDAEIRDL
KNRYLLPAFI DSHNHLSSFG CFFPTWANLI GLTEKEAILK AIRRQVRKEP GTGWIVGFGW
FDARMGGADL TKKDLDEVSS DRPVLLIQTT FHQSVVNTRA LGLLGINQST PDPRCGIIFR
ESDGTPTGVL VEYAQAPVFK LVMEADTETL ADLIEARAKE LLQFGITAIH DPGATPAAEA
AYRQLHAEGR LPVSVLMMPH GETLLDNRLR DRLQGQVTGT GDERLRVGPI KLFADGATAE
TVAFSLKIGG QTINSGCYRD DFEEMLFAAT EKGFRVCVHS FGNATTDAVL TAFENAALRA
PAGFEMRPRL EHVTLINALQ IRRLASMGGC ACIQPQFLSR AQNTKQVMLE DGKWYAYGDL
VKGGVIVASS SDDPGGFMDA RDPIKGSVMG STMSDGEGNV IFPDQVLPFE QWLWMYTAGG
AYAGGQEKER GILKKGMVAD LVILEGSLDS KNPTVVAETW AAGKQVYTKE
//
