ID   A0A0N9UZB6_SPHMC        Unreviewed;       437 AA.
AC   A0A0N9UZB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=AN936_09090 {ECO:0000313|EMBL:ALH80518.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH80518.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH80518.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH80518.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT   Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00001526};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009}.
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DR   EMBL; CP012700; ALH80518.1; -; Genomic_DNA.
DR   RefSeq; WP_054587865.1; NZ_CP012700.1.
DR   AlphaFoldDB; A0A0N9UZB6; -.
DR   KEGG; smag:AN936_09090; -.
DR   PATRIC; fig|33050.5.peg.1887; -.
DR   OrthoDB; 108135at2; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Hydrolase {ECO:0000313|EMBL:ALH80518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..437
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006039180"
FT   DOMAIN          169..268
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   437 AA;  47132 MW;  E026650FBFA4E72A CRC64;
     MRNRWYGLIA AALCAVWLPM TASAQTPETQ SAQTTAFDRR AGELVDLLNG KIAFADYFAP
     SFQQAIPEAQ FKTMTASLIA QYGRAVAVEH ATSKDGRSGT LQLRFEKGIG SVTLDVGADA
     DERVIGLRLT GFQMADDSYD RVAAELAALP GNTGFLVAEL DGAAIRPLAM ANSDKQFAIG
     STFKLYVLDE LAAQIAAGER QWSDVAPLSH LSFSSAGTAN WPKDTPVTLQ TLANWMISVS
     DNGATDTLIH LLGRERIEAR MRAAGHSDPS RNIPFLTTVE AFALKGNNFA DIRPAFIASD
     DKAQRKLIDA NRGRLVLANV DGVSFIDGPR FIDSLEWFAS PNDIARAFIN LRARRSTTLM
     SVLAINNGVG PAAGEPWRYL GYKGGSENGV LSMSLLGERK ADGKWFVVTA SWNDPKANLD
     ADKLVGFVTR LLALAAK
//