ID R5IHY4_9FIRM Unreviewed; 239 AA.
AC R5IHY4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE EC=2.4.1.187 {ECO:0000256|HAMAP-Rule:MF_02070};
DE AltName: Full=N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE AltName: Full=UDP-N-acetylmannosamine transferase {ECO:0000256|HAMAP-Rule:MF_02070};
DE AltName: Full=UDP-N-acetylmannosamine:N-acetylglucosaminyl pyrophosphorylundecaprenol N-acetylmannosaminyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
GN ORFNames=BN480_02161 {ECO:0000313|EMBL:CCY41680.1};
OS Firmicutes bacterium CAG:124.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263002 {ECO:0000313|EMBL:CCY41680.1, ECO:0000313|Proteomes:UP000018269};
RN [1] {ECO:0000313|EMBL:CCY41680.1, ECO:0000313|Proteomes:UP000018269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:124 {ECO:0000313|Proteomes:UP000018269};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-PP-undecaprenol into
CC ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate
CC in the de novo synthesis of teichoic acid. {ECO:0000256|HAMAP-
CC Rule:MF_02070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-
CC beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC trans,octa-cis-undecaprenyl diphosphate + UDP; Xref=Rhea:RHEA:16053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:62959,
CC ChEBI:CHEBI:68623, ChEBI:CHEBI:132210; EC=2.4.1.187;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02070};
CC -!- PATHWAY: Cell wall biogenesis; teichoic acid biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02070}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. TagA/TarA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02070}.
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:CCY41680.1}.
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DR EMBL; CAYD010000160; CCY41680.1; -; Genomic_DNA.
DR AlphaFoldDB; R5IHY4; -.
DR UniPathway; UPA00632; -.
DR Proteomes; UP000018269; Unassembled WGS sequence.
DR GO; GO:0047244; F:N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06533; Glyco_transf_WecG_TagA; 1.
DR HAMAP; MF_02070; TagA_TarA; 1.
DR InterPro; IPR034714; TagA_TarA.
DR InterPro; IPR004629; WecG_TagA_CpsF.
DR NCBIfam; TIGR00696; wecG_tagA_cpsF; 1.
DR PANTHER; PTHR34136; -; 1.
DR PANTHER; PTHR34136:SF1; UDP-N-ACETYL-D-MANNOSAMINURONIC ACID TRANSFERASE; 1.
DR Pfam; PF03808; Glyco_tran_WecG; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02070};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02070};
KW Reference proteome {ECO:0000313|Proteomes:UP000018269};
KW Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944,
KW ECO:0000256|HAMAP-Rule:MF_02070};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02070, ECO:0000313|EMBL:CCY41680.1}.
SQ SEQUENCE 239 AA; 26423 MW; E9BF4DDA84D5BA0B CRC64;
MKLDIMGLQF DNVTMDEASA RAEQILAGKK TCYAVTPNAE IAYEALYDET LRALINGADL
VLPDGAGVVL ASKLLKTPLK QKVAGVDFAD RLLSILEKTG GGLFLLGSKP GVAELAAQKM
TEKHPKLYIC GMNDGYFKDE APVIEKINAA KPDVLFVCLG APKQELFMKN HLDELHIKLM
IGLGGSLDSF AGTVKRAPKW MIRCNLEWLY RLIKEPKRFG RMLRLPKYLF AVLGKRIRG
//
