ID A0A1B1MC27_STRLN Unreviewed; 1072 AA.
AC A0A1B1MC27;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ANS66063.1, ECO:0000313|EMBL:QMV08548.1};
GN ORFNames=GJU35_24850 {ECO:0000313|EMBL:QMV08548.1}, SLCG_3018
GN {ECO:0000313|EMBL:AXG54173.1}, SLINC_3839
GN {ECO:0000313|EMBL:ANS66063.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS66063.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS66063.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS66063.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG54173.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG54173.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV08548.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV08548.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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DR EMBL; CP016438; ANS66063.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG54173.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV08548.1; -; Genomic_DNA.
DR RefSeq; WP_067434946.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1MC27; -.
DR STRING; 1915.SLINC_3839; -.
DR KEGG; sls:SLINC_3839; -.
DR PATRIC; fig|1915.4.peg.4227; -.
DR OrthoDB; 9808778at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
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; 7.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ANS66063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092598}.
FT DOMAIN 932..1017
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 1072 AA; 114600 MW; 28F20395B5329216 CRC64;
MDLEDSSVSS VSSDISVSRR GFLQATVVAG TVAAVGAPAV AAAADSSRTA TTLTFTAATG
GSATLAPSGN RLVVEAQNVL WSVPRSGGTA VALTVPELEP TRPQFSPDGK RLVVCGYRGG
GFHLWTLRAD GSGPRQLTDG PWDDRAPAWS PDGTRIAFAS ERGGDTVTGS PYRVWVLDVR
TGALTRLTGR PGQEGPAQGG AWEDFDPTWS PDGERVLFVR AAVTASGALR ADTVASVAAD
GTGPVTAEHT DTSGAQLMTP AVSPAGRLAY LRTTPSPAAS CRLVVDGTPV AVEGDVQPAP
PRWTDGGRLL LMADGHVRLV DPDAPERGEE IPFTATLPVD RPRYRTKAYD FEGTGTRPVR
ALHLPALSPD GRTVAFVALN ALWTAGTDGH RAPRRILRVP PTRYVTSPAW TPDGKALLYA
DDRDGLFAVR RRDLASGQDT VLAGGGRIFP ALAPDGTRLA CLDISGNLVV RDLAAGTERT
LAAPLGSGGL PGRPSWSPDG RYLALCDRNR LNQRFREGYN LIRVVDTTDG SAVLHPPAPH
TSLSDRYDSG PVWSPDGRWM AVVAESALWL LPVRADGTPD GEPRRLTSEP ADHPSWSADS
RTLLYLSAGT PRLADLASGT TRTVRIRLDY RRPRPADTVV RAGRFWDGTG TEVREDVDVV
IRDGRIAEVA PHRTARPAAR RVDASERTVV PGLWDAHTHP WQTTYGGRQT ALQLAYGITT
AVSLGGFAYE QARIREAVAS GELAGPRLLS TGELLDGSRV AYSMGRAHRT REGLRRSLER
AAALDWDFVK TYVRAPGWVM KEAADFAHHR LGVRSGSHLC TPGVQLGQDL TTHLQATQRL
EFGHATTAAG NAFQDVEEIY TRTDFHLVAT PFTALPLLGA DPSLAEDPRV TTLMPPWDTA
MVRQLATQPP SVLQLATLDR ELGFYRRVLA GGGLVALGTD QPLVPVGLHL HLGLRALHRA
GLSPAEALRT ATLLPARVFG ADTDLGTLEE GKLADLTLVD GDPFTDFTDL IRTRAVLRGG
VLFEQSDLVG AFDAATARTD PKEPADPTTD EDWLEVSRHM RREGCCDPGT GY
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