ID A0A1X1QQD0_9GAMM Unreviewed; 475 AA.
AC A0A1X1QQD0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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 Name=cpsB {ECO:0000313|EMBL:ORU93377.1};
GN ORFNames=A6F70_05460 {ECO:0000313|EMBL:ORU93377.1};
OS Cycloclasticus sp. symbiont of Bathymodiolus heckerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1284675 {ECO:0000313|EMBL:ORU93377.1, ECO:0000313|Proteomes:UP000193616};
RN [1] {ECO:0000313|EMBL:ORU93377.1, ECO:0000313|Proteomes:UP000193616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Specimen P {ECO:0000313|EMBL:ORU93377.1};
RA Rubin Blum M., Dubilier N.;
RT "Short-chain alkanes fuel the metabolism of mussel and sponge
RT Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL Submitted (APR-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 -!- 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 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:ORU93377.1}.
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DR EMBL; LWTL01000115; ORU93377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1QQD0; -.
DR STRING; 1284675.A6F70_05460; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000193616; 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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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:ORU93377.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ORU93377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193616};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ORU93377.1}.
FT DOMAIN 4..292
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 320..470
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 475 AA; 52189 MW; C222E5272D7614FB CRC64;
MILPVIMAGG SGSRLWPLSR QLFPKQFLPL VGDETMLQST CSRLEGLAHH APLLICGEDH
RFTVAEQLRT SGHANSPIIL EPAGRNTAPA VALAALHAIK EGDDPVLLVL AADHVIADVN
AFQASVSTAL PFAEQGKLVT FGIVPTAAET GYGYIQRGAV RESGAFDVAE FVEKPDLATA
EQYLSRGEFY WNSGMFMFKA SRYLEVLKEQ QLDIYKACEQ AMTNAAVDSD FIRPDKEIFL
SCPDDSIDYA VMEPLCSTAA SGDDVVVVPM ECGWSDVGSW SALWDVSEKD ENGNTCKGDV
LSHDTQNCFI QSDGKLIATV GLDGIVVVES DDAIMVAAKD RVQDVKKIVE TLKAQERSEA
TVHRKVYRPW GFYDSIDQGE RFQVKRIVVS PGAQLSLQMH HHRAEHWIVV SGTAKVTKGD
EVFLLAENES TYIPLGVTHR LENSGSIELE MIEVQSGSYL GEDDIVRFED NYNRE
//
