ID A0A849FU13_9RHOB Unreviewed; 386 AA. AC A0A849FU13; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 24-JUL-2024, entry version 9. DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:NNK78089.1}; GN ORFNames=HKP40_05180 {ECO:0000313|EMBL:NNK78089.1}; OS Litoreibacter sp. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Litoreibacter. OX NCBI_TaxID=1969459 {ECO:0000313|EMBL:NNK78089.1, ECO:0000313|Proteomes:UP000554301}; RN [1] {ECO:0000313|EMBL:NNK78089.1, ECO:0000313|Proteomes:UP000554301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Site_B17 {ECO:0000313|EMBL:NNK78089.1}; RA Chen Y.-J., Leung P.M., Cook P.L.M., Wong W.W., Kessler A.J., Greening C.; RT "Hydrodynamic disturbance controls microbial community assembly and RT biogeochemical processes in coastal sediments."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR005962-1}; CC Note=The Mn(2+) ion enhances activity. {ECO:0000256|PIRSR:PIRSR005962- CC 1}; 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:NNK78089.1}. 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; JABDPP010000167; NNK78089.1; -; Genomic_DNA. DR AlphaFoldDB; A0A849FU13; -. DR Proteomes; UP000554301; Unassembled WGS sequence. DR GO; GO:0010179; F:IAA-Ala conjugate hydrolase activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009850; P:auxin metabolic process; IEA:TreeGrafter. DR CDD; cd05666; M20_Acy1-like; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR NCBIfam; TIGR01891; amidohydrolases; 1. DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1. DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 4: Predicted; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:NNK78089.1}; KW Manganese {ECO:0000256|PIRSR:PIRSR005962-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR005962-1}. FT DOMAIN 188..283 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" FT BINDING 104 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005962-1" FT BINDING 106 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005962-1" FT BINDING 139 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005962-1" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005962-1" FT BINDING 358 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005962-1" SQ SEQUENCE 386 AA; 41908 MW; 466766A8395508F6 CRC64; MPVKNRFAEL LPEITEWRRD LHENPEILFE THRTSALVAE KLKEFGCDEV ETGIGRTGVV GVIKGKSDNS GKTIGLRADM DALPILEATG LDYASKTPGA MHACGHDGHT AMLLGAAKYL AETRNFDGTV VVIFQPAEEG GGGGREMCED GMTDRWSIDE YYGMHNWPGM PVGSFHIRPG PFFAATDTFD IHVEGRGGHA AKPHETIDTT VAASNMVMAL QSIVSRNADP VQQIVVSVTS FETESKAYNV IPQHVHLRGT IRTLTPEARA LGEKRLKEIA EASANVYGAT ARVEFHPGYP VMTNWEEPTE FAAAVASRVS GSCGEAPLVM GGEDFAYMLE ERPGAYILVG NGETAPVHHP GYNFNDETIP AGCSWWAEIV EQRLPA //