ID   C0L631_MYCGL            Unreviewed;       938 AA.
AC   C0L631;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
OS   Mycoplasmoides gallisepticum (Mycoplasma gallisepticum).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=2096 {ECO:0000313|EMBL:ACN39721.1};
RN   [1] {ECO:0000313|EMBL:ACN39721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F {ECO:0000313|EMBL:ACN39721.1};
RX   PubMed=19329630; DOI=10.1128/JB.00142-09;
RA   May M., Brown D.R.;
RT   "Diversifying and stabilizing selection of sialidase and N-
RT   acetylneuraminate catabolism in Mycoplasma synoviae.";
RL   J. Bacteriol. 191:3588-3593(2009).
RN   [2] {ECO:0000313|EMBL:ACN39721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F {ECO:0000313|EMBL:ACN39721.1};
RA   May M.A., Brown D.R.;
RT   "Sialidase activity in Mycoplasma gallisepticum.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FJ659842; ACN39721.1; -; Genomic_DNA.
DR   RefSeq; WP_014574495.1; NZ_CP028147.1.
DR   AlphaFoldDB; C0L631; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   938 AA;  108058 MW;  8BA4C37947270426 CRC64;
     MKKTKAQKDQ QKKSQFKKRF WFTFTFLIGS ITIISSFLIP LSLKWIWAPL NIEEDLEINI
     KDDLNGSRFI SEINSDNLPE FVNAFFNNKQ YSIDDLNLKL AGVNYITGWV YVQASVKPNV
     KVAKKYQDAV KLFKLEFKNS QVKLFDPNVT TFLIKPENNT KEFTSEFQTR EDLESFLNNA
     DNISLSELQD KLNLTFFDKN NVPLNLYTGA VVTLSNPVKF TIASYVMDYK ITWQIPAAND
     VFYGNLYPFS LNGKLNLWLK KINSISSLYS DVDDIDFKKL QSKEIFRNLE EVQNFSTSIE
     TLDQFYNAPD DLVVKGQDFK LGYYVNKTAQ TFDNVESFLD NSNLISSGYL TRMTYDDKHK
     VVISKPNLDT FTKASSETQR KYLQSFKQNK APVKVTIANT VDRTVEVFYT DFSFNKSPLV
     NGKYLFFNMS PPGDKFVYYT KDVNTWRIPG VVKTHDNKLI FNADKRVNNK DDRGHLEQDI
     RVSEDGGKTW SNPQTIVRIS AKNTKDGANK GQVIDGTMLE VFDKSINKHK LLYVFGVSSY
     LHTVHDEWTI RGDGNTSGLV NNNKWMLFID KENLNQKFVA KPITVDGDSN WFKVFKVKNS
     SRVQWKDIDD TTQLDEANII IDNSLKNGTI TGNVYDKVPS NIFSTFGEPG RNSRSSEISG
     YISKYSIWDQ RWPNYFVFNR MQKNAYFANS RYYFDNILWT FQVESIDGGK TWTNLRNVSP
     FLNRKDQRWY INGVGNGIQL NHQRNSNGDV IAVFPFYFAN KRKLERSKLM ATKDGGKTWY
     ELADYPFKLL PPGASESSIS EDSKGNLWWL ARRSDGRVFT LIKSEDGGKN WKVIFNAKRG
     IFTGQFIGST IFNIKALGEK LIFSASDNRG GKIYLVDINN PRTLEPIYTI NRGSYGYSTT
     VTFNENDNYF DVLTFYEVNS PQKGRDINLK RLRVFVVS
//