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Database: UniProt
Entry: A0A4R1ALL9_9ACTN
LinkDB: A0A4R1ALL9_9ACTN
Original site: A0A4R1ALL9_9ACTN 
ID   A0A4R1ALL9_9ACTN        Unreviewed;       630 AA.
AC   A0A4R1ALL9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:TCI97616.1};
GN   ORFNames=E0W78_11225 {ECO:0000313|EMBL:TCI97616.1};
OS   Aeromicrobium sp. IC_218.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2545468 {ECO:0000313|EMBL:TCI97616.1, ECO:0000313|Proteomes:UP000293071};
RN   [1] {ECO:0000313|EMBL:TCI97616.1, ECO:0000313|Proteomes:UP000293071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IC_218 {ECO:0000313|EMBL:TCI97616.1,
RC   ECO:0000313|Proteomes:UP000293071};
RA   Johnsen N., Bonefeld L., Nazipi S., Marshall I.P.G., Schramm A.;
RT   "High quality draft genome sequence of Aeromicrobium massiliense IC_218,
RT   isolated from nest material.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC       sulfatase family. {ECO:0000256|ARBA:ARBA00033751}.
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:TCI97616.1}.
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DR   EMBL; SJXM01000009; TCI97616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R1ALL9; -.
DR   OrthoDB; 5240502at2; -.
DR   Proteomes; UP000293071; Unassembled WGS sequence.
DR   GO; GO:0018741; F:linear primary-alkylsulfatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0018909; P:dodecyl sulfate metabolic process; IEA:InterPro.
DR   CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR   Gene3D; 1.25.40.880; Alkyl sulfatase, dimerisation domain; 1.
DR   Gene3D; 3.60.15.30; Metallo-beta-lactamase domain; 1.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR   InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR   InterPro; IPR029229; Alkyl_sulf_C.
DR   InterPro; IPR029228; Alkyl_sulf_dimr.
DR   InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   PANTHER; PTHR43223; ALKYL/ARYL-SULFATASE; 1.
DR   PANTHER; PTHR43223:SF1; ALKYL_ARYL-SULFATASE BDS1; 1.
DR   Pfam; PF14864; Alkyl_sulf_C; 1.
DR   Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:TCI97616.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000293071};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          103..325
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   630 AA;  67662 MW;  2C24A950AEEE5DC4 CRC64;
     MTTAPKDASP AVVAQQRAVL DTLPFSDVRD FDAVRRGLVA RREPNAVTAE DGRVVWDNDT
     YGFLTGDAPD TVNPSLWRQS TLVAADGLFE VVPGVYQVRG LDLSNISFVE GDTGVIVIDP
     LISTETAAAA LDLYREHRGD RPVTGVIYTH SHVDHFGGVK GVTSQEDVDA GRVPVLAPEG
     FVEHAVAENV YAGTAMGRRA GYMYGAALPR SPRGALGAGL GQTTSTGTVT LIAPTVEITT
     TGQEEVVDGV RIVFQMAPDT EAPSEMLFYF PDLKALCAAE DATHTLHNLL TLRGALVRDP
     HVWSTYLTET LDLFGAEVEI VFASHHWPTW GNADVVEFLT LQRDLYAYLH DQTLRMLNQG
     LTGSEIAEQI TLPPALEDAW STRGYYGSVS HDVKAIYQRY MGWFDGNPAH LWEHTPVEKA
     VRYVALGGGA DAVVAHGRDA LEAGDLRWAA EVLSHVVFAE PDHPTARELL ADTLEQLGYG
     AENGTWRNFY LSGAYELRNG GFGTPTVTAS PDMVAELSPG MLFDALAVQV DGPAAWDERL
     TIDVVLTDAD ERYRLRLAHG VLVHSAAPQT GAPDATLTTT RRGLTALATG PLTSERLTAA
     GIAVDGDASA LTRLAAVLDP GDPDFAIVTP
//
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