ID C9KN46_9FIRM Unreviewed; 628 AA.
AC C9KN46;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Hyaluronan synthase {ECO:0000256|ARBA:ARBA00040508};
DE EC=2.4.1.212 {ECO:0000256|ARBA:ARBA00012207};
DE AltName: Full=Hyaluronate synthase {ECO:0000256|ARBA:ARBA00043237};
DE AltName: Full=Hyaluronic acid synthase {ECO:0000256|ARBA:ARBA00042148};
GN ORFNames=MITSMUL_04857 {ECO:0000313|EMBL:EEX68785.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68785.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX68785.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68785.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosaminoglycan synthesis. The hyaluronic acid capsule is
CC involved in the pathogenicity of group A Streptococci; it may be the
CC major virulence determinant. {ECO:0000256|ARBA:ARBA00037408}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-
CC alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP;
CC Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC Evidence={ECO:0000256|ARBA:ARBA00001330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-
CC acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP;
CC Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC Evidence={ECO:0000256|ARBA:ARBA00000790};
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004698}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family.
CC {ECO:0000256|ARBA:ARBA00006782}.
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:EEX68785.1}.
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DR EMBL; ABWK02000017; EEX68785.1; -; Genomic_DNA.
DR RefSeq; WP_005841750.1; NZ_GG697142.2.
DR AlphaFoldDB; C9KN46; -.
DR STRING; 500635.MITSMUL_04857; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 78516293; -.
DR PATRIC; fig|500635.8.peg.1547; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_029695_4_2_9; -.
DR Proteomes; UP000003671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0050501; F:hyaluronan synthase activity; IEA:RHEA.
DR CDD; cd06423; CESA_like; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
DR PANTHER; PTHR22913; HYALURONAN SYNTHASE; 1.
DR PANTHER; PTHR22913:SF12; N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF07238; PilZ; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EEX68785.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EEX68785.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..162
FT /note="PilZ"
FT /evidence="ECO:0000259|Pfam:PF07238"
FT DOMAIN 244..422
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 72965 MW; DC2C9A79F7AC07BE CRC64;
MANDKKKTSV EDDVLFRLKP DRRLLSYAPD VTGHRTNRDR RGRDSADTGT SSGYIKLQQD
DKNGQRYLVN YSVTVRFTLH GQKKSVQMKG EDISTTGILL TTPSSAEQVP LMEAEDVRLT
FEITPGSMPE GYEMMVRKIP ATCVREASRP DGAHLYGMQF KSTLAEFSNT HRKNYMLAVA
SFFLAVIVFV IVLMRAESVI YFQFNRWLYL YSIIAATFLL TRYLFGSFYR PTKIDPDYTP
GVMIIVPCFN EEKWIQHTIL GCINQDYPID KLEVIVVDDC SNDHSVDKIK EIIERLKQSD
GDQKMYRVED RLHYYVQPVN KGKREAMAVG AHMAKHELLV FVDSDSFLDP YAVRNIVQPF
KDKKMGGVSG RTDVANTYTN SLTKMQAVRY YIAFRIMKAA EGYFDAVTCL SGPLSCYRKD
LVLKYCDDWL NQKFLGQRAT FGDDRSMTNF ILRHHRTTYQ DTAVCMTIVP KSHKMFLRQQ
MRWKRSWLRE SIIAARYMWK KEPFMALSFY MGLLVPIAAP IIVLYNLIYI PIMHRVFPLT
FLVGMLMMAL LMSMAQLFLR RSTTWIFGVW FCLYYEAVLL WQMPVAWFTF WKSTWGTRLT
PADLAEIEKA KKKQQKKVRR EGKKVDEH
//
