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Database: UniProt
Entry: A0A1G8E1H1_9RHOO
LinkDB: A0A1G8E1H1_9RHOO
Original site: A0A1G8E1H1_9RHOO 
ID   A0A1G8E1H1_9RHOO        Unreviewed;       491 AA.
AC   A0A1G8E1H1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN   ORFNames=SAMN05660652_01998 {ECO:0000313|EMBL:SDH63529.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDH63529.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDH63529.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDH63529.1,
RC   ECO:0000313|Proteomes:UP000198607};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC       {ECO:0000256|ARBA:ARBA00006115, ECO:0000256|RuleBase:RU004190}.
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DR   EMBL; FNCY01000007; SDH63529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8E1H1; -.
DR   STRING; 83767.SAMN05660652_01998; -.
DR   OrthoDB; 9806359at2; -.
DR   Proteomes; UP000198607; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd02213; cupin_PMI_typeII_C; 1.
DR   CDD; cd02509; GDP-M1P_Guanylyltransferase; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR049577; GMPP_N.
DR   InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR   InterPro; IPR001538; Man6P_isomerase-2_C.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR01479; GMP_PMI; 1.
DR   PANTHER; PTHR46390; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR46390:SF1; MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF01050; MannoseP_isomer; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Isomerase {ECO:0000313|EMBL:SDH63529.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:SDH63529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198607};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDH63529.1}.
FT   DOMAIN          6..304
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          334..484
FT                   /note="Mannose-6-phosphate isomerase type II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01050"
SQ   SEQUENCE   491 AA;  53190 MW;  B26B23E21FAF3462 CRC64;
     MYSVTPVILC GGSGTRLWPL SRSGFPKQFL CLTGEDSLFQ QAAQRLVGLG GNDVQVEKML
     IVSGEEHRFL VTEQLREAGI ALGAALLEPK GRNTAPALTL AALAALEDGK DPVLVVTPAD
     QTVADSAAFT ASMQAAIRAA AAGSIVILGI SPDRPETGYG YIQTDSAVGT SADEQTALRA
     VQRFVEKPDA ATAQRYLDAG GYYWNAGMFV LKASVWMKAL ERFRPDIAVS TRAAWTQRSA
     DIGAMTPFVR PDKDAFIAIP SESVDYAVME RCPGSEFDIR MVPLDAGWSD LGAWDAVWQV
     LPKDDAGNAS VGDVMTTACE NTLVHAASRL VALVGVKDVV VIETSDAVLV ADRARSQDVK
     AIVNDLAARG REEYALHRKV HRPWGWYDSI DEGGRFKVKR IQVKPKASLS LQKHHHRAEH
     WIVVKGTAEI TNGDKTMLIT ENQSTYIPLG EVHRLANPGT IPLEIIEVQS GSYLGEDDIV
     RFEDSYGRSK A
//
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