ID A0A1Y4M1S6_9FIRM Unreviewed; 671 AA.
AC A0A1Y4M1S6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|RuleBase:RU367007};
GN ORFNames=B5F12_11015 {ECO:0000313|EMBL:OUP62130.1};
OS Pseudoflavonifractor sp. An176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=1965572 {ECO:0000313|EMBL:OUP62130.1, ECO:0000313|Proteomes:UP000196146};
RN [1] {ECO:0000313|Proteomes:UP000196146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An176 {ECO:0000313|Proteomes:UP000196146};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|RuleBase:RU367007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367007}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|RuleBase:RU367007}.
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:OUP62130.1}.
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DR EMBL; NFKO01000044; OUP62130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4M1S6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000196146; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR032421; PMT_4TMC.
DR InterPro; IPR038731; RgtA/B/C-like.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF13231; PMT_2; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000196146};
KW Transferase {ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 303..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 366..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 403..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 444..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 551..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 575..592
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 598..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 629..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 290..430
FT /note="Glycosyltransferase RgtA/B/C/D-like"
FT /evidence="ECO:0000259|Pfam:PF13231"
FT DOMAIN 491..669
FT /note="Protein O-mannosyl-transferase C-terminal four TM"
FT /evidence="ECO:0000259|Pfam:PF16192"
SQ SEQUENCE 671 AA; 76720 MW; E2CEAFD5585ABB06 CRC64;
MELFTAATAT SSASPNLFER IQQGWDSAVT GVGWFFTNLS PAFVFALMGM AIVVAFFVYY
WYCLKPRANS LEWIAMSEAQ SRRKSMSLTL PYTPMERCDW IPLMLVTVIY AITAFFQLGS
MSAPESYVKF QQGDSYTFSF SQPVKVDEIS FYTSLGTGTY RLEYTNNGSD WKWVDLDQNY
ATLFKWETVD LNQIPEGMDV PPVTLEATTF RITATTADRT EGVWLAELAL WSDGEPLIPD
HVDVGAEALF DEPEEWTTKQ TYRNSSYFDE IYHPRTALEH LNNIYPYEVS HPPLGKLIMS
IGIALFGMVP FGWRFMGTLF GVLMLPILYV FLKNFFGKTP VAFCGTCLFA FDFMHLVQTR
IGTIDTYGVF FILVSYYFMY RWLCCPVGSS LRKTAVPLFL CGLFWGIGCA CKWTVIYAGA
GLAVMWLLGL VFRYREWKLA PQGFDFISFV LSTTSLSIIF FVLLPSVIYT ASYIPYATAQ
GNLTLDNLLN VMWSNQEFML SYHQGVHSTH PYQSSWYQWI FDARPILYYR DLDLANTEGV
KSLFASFNNP LVSWAGLLAF FAVLIQTIRR KCGRGLFILI AILSQFLPWL PIGRTLFAYH
YFPTILFLVF AIAYLMNDML DRHKKGATLA VYGFTGCTVA VYAIFYPALT GLYIPLWYSE
VFLRWFPSWP L
//
