ID A0A1Q5L9Q0_9ACTN Unreviewed; 1048 AA.
AC A0A1Q5L9Q0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OKJ91046.1};
GN ORFNames=AMK33_35880 {ECO:0000313|EMBL:OKJ91046.1};
OS Streptomyces sp. CB02400.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKJ91046.1, ECO:0000313|Proteomes:UP000185993};
RN [1] {ECO:0000313|EMBL:OKJ91046.1, ECO:0000313|Proteomes:UP000185993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02400 {ECO:0000313|EMBL:OKJ91046.1,
RC ECO:0000313|Proteomes:UP000185993};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ91046.1}.
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DR EMBL; LIWB01000024; OKJ91046.1; -; Genomic_DNA.
DR RefSeq; WP_073937381.1; NZ_LIWB01000024.1.
DR AlphaFoldDB; A0A1Q5L9Q0; -.
DR Proteomes; UP000185993; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07676; PD40; 5.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:OKJ91046.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185993}.
FT DOMAIN 675..996
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1048 AA; 111610 MW; 25CAE788342D50FA CRC64;
MSSGSVSRRG FLGVSAAGLT GALSPVATRA EAASAAGEDQ VLRYEEMTGG SVTASRDGKL
LIAEVQGVLW RVPRGGGAAT RLTDWELEAT APALSPDGGT VALCGYRDGT FHLWTMGADG
SGLRRLTDGP WDDRGPAWSP DGTRLVFSSE RGGDAVAGSA FGLWVLDVRD GRVRRLTGGD
FEDLDAAWCP DGRSVVCVRA AHTPDGASDG GRALVRVPAA GGEARVVHSV GSGRLLCPSV
SPAGRIACLR LSGTGSSPSL PAAKAVLMVD GRVVTDDEDL AAAPPCWLDE DRLLYVADGR
IRIRTLDSSA PVEEVAFTAR MPMPRPRRRV GPRNRYPARP VPVRGIHLPA LSPDGGSVAF
VALNALWLMD VGGAPRKLVQ ASPVHHLQMP VWAPDGRTLL YCTDRDGLTA VRRLRPDDGH
DEPVTGQGRL CPALSPDGTL LACQDVTGNL LLRTLATGAE RVLARPMATD GPPGAPTWSP
DGRYVAFCDR NRLNHRFREG YHLIRVVDTR TGAERRHLPA DHQSLADRAA AGPVWSPDGR
WMALIAESAL HLLPVTADGT PAGPVRRLTD EPADHACWAG DSATLLYLSS GRLRLLSLDE
ERVPSRTRTL PVLLTTGQRP RHEPLRVHAG RLWDGTGTTV RQDVDILVEG GRITTVEPHR
ARRPGHRTLD ASDHTVVPGL FDSHTHPYTA TYGARQHLAA LAYGITTTAC MGAPLYEAVR
LRESLAAGHS TGPRMLACAE LIDGPRTAYA KGRAHRTHAG LRRTLERVTA LDADFVKTYV
RAPGRAMAEA AEAAHRLGVP CGSHLCSPGR AAGQDLTTHL QATQRLAYGH ATTPTGHLHQ
DLLEQYADGS FALIATPFTA QALLGADPAL ADDPRVLALL PPWDVAAVQE RAKTEPTAEQ
RRALAIEMGN YRRLAAHGAT LALGTDSPLV PVGLSLHLAL RALVAHGFTP VQALRTVTTT
PARLFGLDAD LGTVEPGRIA DLTVVDGDPF TDFAALVDIP LVLRDGVPHR QADLTATHRQ
APAPAPRNTT WLEVAHTLHR NSCCHSGD
//