ID E6SGT2_THEM7 Unreviewed; 380 AA.
AC E6SGT2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADU51666.1};
GN OrderedLocusNames=Tmar_1557 {ECO:0000313|EMBL:ADU51666.1};
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS 7p75a).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51666.1, ECO:0000313|Proteomes:UP000008915};
RN [1] {ECO:0000313|EMBL:ADU51666.1, ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX PubMed=21304738;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75a).";
RL Stand. Genomic Sci. 3:337-345(2010).
RN [2] {ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002344; ADU51666.1; -; Genomic_DNA.
DR RefSeq; WP_013495969.1; NC_014831.1.
DR AlphaFoldDB; E6SGT2; -.
DR STRING; 644966.Tmar_1557; -.
DR KEGG; tmr:Tmar_1557; -.
DR eggNOG; COG3964; Bacteria.
DR HOGENOM; CLU_036699_2_0_9; -.
DR Proteomes; UP000008915; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; DIHYDROOROTASE-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008915};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT DOMAIN 83..341
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 158
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 380 AA; 40488 MW; B9FDFFB68CAA1BC5 CRC64;
MKVDLAIRGG RVIDPATGLD REGTVLVSDK RILAIEAPDA AVEAERVIDA RGLLVLPGLI
DLHAHCFVGE TRLGLPPDRI GVQQGVTTVV DAGSSGVDNL LRFRESVRGA RTRVLAYINL
ARDGLARHRG ELADPRMLAP DETVEALRAH GGFLVGVKAR ASASVVGDQG IAPVRLAKET
AKRAGVPLMV HIGNAPPRLE EVLELLEAGD IVSHAFHGKK GGIYRDGTLL PEARAALERG
VLFDVAHGQA SFSYATCRRF LADGLVPHII SSDLWRGNET GPVVSLLHCM SKLLHLGMPL
QEVVAATTWR PAVALHRQHE IGSLAPGRIA DISIIRQVRG QFPLQDSEGV TEVVSCLLEP
VMTIRHGHIV GDIGPGGISA
//
