ID A4QED4_CORGB Unreviewed; 909 AA. AC A4QED4; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 24-JAN-2024, entry version 78. DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733}; DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733}; GN OrderedLocusNames=cgR_1608 {ECO:0000313|EMBL:BAF54600.1}; OS Corynebacterium glutamicum (strain R). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=340322 {ECO:0000313|EMBL:BAF54600.1, ECO:0000313|Proteomes:UP000006698}; RN [1] {ECO:0000313|Proteomes:UP000006698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R {ECO:0000313|Proteomes:UP000006698}; RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0; RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.; RT "Comparative analysis of the Corynebacterium glutamicum group and complete RT genome sequence of strain R."; RL Microbiology 153:1042-1058(2007). 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; AP009044; BAF54600.1; -; Genomic_DNA. DR AlphaFoldDB; A4QED4; -. DR KEGG; cgt:cgR_1608; -. DR HOGENOM; CLU_317070_0_0_11; -. DR Proteomes; UP000006698; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt. DR CDD; cd15482; Sialidase_non-viral; 1. DR Gene3D; 2.120.10.10; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR018905; A-galactase_NEW3. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011040; Sialidase. DR InterPro; IPR026856; Sialidase_fam. DR InterPro; IPR036278; Sialidase_sf. DR PANTHER; PTHR10628; SIALIDASE; 1. DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1. DR Pfam; PF13088; BNR_2; 1. DR Pfam; PF10633; NPCBM_assoc; 1. DR SUPFAM; SSF50939; Sialidases; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..29 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 30..909 FT /note="exo-alpha-sialidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002672527" FT TRANSMEM 886..907 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 97..382 FT /note="Sialidase" FT /evidence="ECO:0000259|Pfam:PF13088" FT DOMAIN 418..488 FT /note="Alpha-galactosidase NEW3" FT /evidence="ECO:0000259|Pfam:PF10633" FT REGION 849..882 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 853..870 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 909 AA; 96616 MW; A76B8223D31BD78F CRC64; MSRRKAVFSA LGAAALIGAA LPTIPTAQAQ TPTGYGFDAT ASIGEEPEFS TQQLADGGTL GFDCYRIPSL GVAPNGNVLA SWDGRPNNCS DAPQPNSIVG KVSTDNGATW GEQHDISAGI TAEPKTGYSD PSIVVDWERG DVFNFHVKSF DAGYFTSQPG TDPDDRNVAH VAYAKSSDNG STWVADTVIT DQVVADDTWD SRFATSGNGI QLQYGAYKGR LVQPSVTRMT NGRVAAVAML SDDHGTTWYP SAPWGNSMDE NKIVELSDGT LMNNSRSSGA DTYRKVSYST DGGVTWTEPT LDTQLPDPRN NASLIRVFPT APEGSAQAKV LLFSNTATTS GRTNGTVRMS CDDGQTWPVS KVFEPGAIQY TSMATLPNGD IGMLWENSGS NIDIFYSQFN LSWLEAGCIG VDADETPVTA GETTTMNVTL TNPFANAIFD RAVSLELPEG WQAEDVRVSI PSGESVTIPV QVTAPLVADN GELPVEVSIL DGADRYTGRL NLTVQGGQEP ASTSVKVSIP NLKDTYVAGE KISINFAVNN PFDVTVNSVP SLGEGENWMP ANLRGFDPEQ GAPNCRYRNL GANQSYNCTT TTYEVSDSDV ERGYVDIPTV WTFTNSAGET VWSKNVDVPR IELNGTQDAV TDAIVTVDPI NPVHSNGQSQ TVEVQANVTS EGDLPAGSKV AFYLDSSPID AAAVDAEGHA SISIDVDNIA SEQPERTFEV RARLVVPEDA PRSIARDALA RFTVLPEQVQ QNSLVIMNHP DVVSDGQTKT IVIAVKATAH DGSPVAIGTL ITFRVNGIER DVVPTNAQGT AKLQLDLKPV NTEDEEYEVT VEAELDELTA QTTFKVLAGE EEEPTSTEEQ PSETEQPSEP EEEPTAPTGS SNGGSFAALL ALLAALGGIV GAVLGLLKL //