ID C3X8Y5_OXAFO Unreviewed; 312 AA.
AC C3X8Y5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=OFBG_00689 {ECO:0000313|EMBL:EEO29661.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO29661.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO29661.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO29661.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; GG658170; EEO29661.1; -; Genomic_DNA.
DR AlphaFoldDB; C3X8Y5; -.
DR STRING; 847.BRW83_1540; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_031960_0_1_4; -.
DR Proteomes; UP000005089; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000005089}.
FT DOMAIN 37..261
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 312 AA; 34058 MW; C4E6613528F8CD17 CRC64;
MSTLLASFTL VTASCLASPL QENIDAIVKD KPAQIGVVIE GFDPHQHAGF NENTRFPMQS
VFKFPVALAV LDQVDKGKIN LDETLLLKPS DLLPNTHSPL REKYPEANAA VSIGEIINET
VSNSDNNGCD ILLRLVGGPQ AVDQYIKNLG IADMQIAVNE QEMHTVKDAQ HKNWTTPAAM
TQLLRLFHDG KLLKPDSQKF LWTAMRDSVT APGRLRSPLP AGTHLIHKTG TSDYSPQDGS
TVNDVGIILL PDGNPVFISV LISGSKMSMM DTEKIIASVS GVAWDHFSQE KPGLSIRKTG
KQLRELIGFE NQ
//
