ID D4B1M6_ARTBC Unreviewed; 426 AA.
AC D4B1M6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000256|ARBA:ARBA00018601};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
DE AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031190};
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030179};
GN ORFNames=ARB_02355 {ECO:0000313|EMBL:EFE30865.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE30865.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000256|ARBA:ARBA00024813}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001083};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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:EFE30865.1}.
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DR EMBL; ABSU01000026; EFE30865.1; -; Genomic_DNA.
DR RefSeq; XP_003011505.1; XM_003011459.1.
DR AlphaFoldDB; D4B1M6; -.
DR STRING; 663331.D4B1M6; -.
DR GeneID; 9523273; -.
DR KEGG; abe:ARB_02355; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_0_0_1; -.
DR OMA; GPNCWIC; -.
DR OrthoDB; 5486038at2759; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd05824; LbH_M1P_guanylylT_C; 1.
DR CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR045233; GMPPB_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 397..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..236
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 426 AA; 46734 MW; A4F81E2303A55B75 CRC64;
MKALILVGGF GTRLRPLTLT LPKPLVEFAN RPMILHQVES LAAAGVTDIV LAVNYRPDVM
VSALKKVASP QYLSPLDGDA KGANMNRSTA GPLKLAEKIL GKDDSPFFVL NSDVICEYPF
QALADFHKAH GDEGTIVVTK VEEPSKYGVV VHKPNHPSRI DRFVEKPVEF VGNRINAGIY
ILNPSVLKRI ELRPTSIEQE TFPAICKDGQ LHSFDLEGFW MDVGQPKDFL SGTCLYLTSL
TKQGSKLLAS PSEPYVHGGN VLVDPSAKIG KNCRIGPNVT IGPNVVIGDG VRLQRCVLLA
NSKVKDHAWV KSSIIGWNSS VGRWARLENV SVLGDDVTIG DEVYVNGGSI LPHKSIKQNV
DCLLLHLHMI IKKSTSLHNL QLGRYEVRGH DHRSDGWVLF LLCSGLLFYL NFLLLSSCSL
MAHFSC
//
