ID A0A1Q3VPB9_9PROT Unreviewed; 470 AA.
AC A0A1Q3VPB9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN ORFNames=BGO63_03210 {ECO:0000313|EMBL:OJW48269.1};
OS Candidatus Accumulibacter sp. 66-26.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1895689 {ECO:0000313|EMBL:OJW48269.1, ECO:0000313|Proteomes:UP000186203};
RN [1] {ECO:0000313|EMBL:OJW48269.1, ECO:0000313|Proteomes:UP000186203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=66-26 {ECO:0000313|EMBL:OJW48269.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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}.
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:OJW48269.1}.
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DR EMBL; MKUH01000025; OJW48269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3VPB9; -.
DR STRING; 1895689.BGO63_03210; -.
DR Proteomes; UP000186203; 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:OJW48269.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:OJW48269.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OJW48269.1}.
FT DOMAIN 2..278
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 313..463
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 470 AA; 51040 MW; 6AC553EA53D6983D CRC64;
MPTILCGGAG TRLWPVSREL HPKPFIRLAD GQSLLQKAYL RGAQLPGVNH LMTVTNRELF
FKTEDEFREV NATQASTAFI LEPFGRNTAP AIAAAALQVA ATHGPDAILL ILAADHLISD
QTGFEQAVVN AVELAQQGKL VTFGIQPDTA ETGYGYIESE GNRVLRFVEK PSLEKAQSYL
ASGRFLWNSG MFCFAAGAIL GQMEKHCPAI LTATQACIEQ SRLATGDGFS QLELDANAFQ
TVPDNSIDYA VMEKSDQVAV VPCSIGWSDI GSWAALGDLG AVDACGNRIQ GEAILHNTRN
CTIQSDGRLV GAVGVDNLII IDTPDAVLVA NKAHAQDVKH IYAELKAQGH EAHKLHRTVH
RPWGTYTVLE EDDGFKIKRI EVKPGASLSL QMHHHRSEHW VVVSGFAKVI NGDHEILINT
NESTFIPAGH KHRLTNSGPT SCVMIEVQCG KYVGEDDIVR FEDSYGRISA
//
