ID A0A0C4WJ84_9GAMM Unreviewed; 481 AA.
AC A0A0C4WJ84;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00012387};
DE EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
GN Name=algA {ECO:0000313|EMBL:AJE22538.1};
GN ORFNames=Achr_31290 {ECO:0000313|EMBL:AJE22538.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE22538.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE22538.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE22538.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
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}.
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DR EMBL; CP010415; AJE22538.1; -; Genomic_DNA.
DR RefSeq; WP_039805755.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WJ84; -.
DR STRING; 1328314.Achr_31290; -.
DR KEGG; acx:Achr_31290; -.
DR HOGENOM; CLU_035527_1_0_6; -.
DR UniPathway; UPA00126; UER00930.
DR Proteomes; UP000068210; Chromosome.
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; IPR018247; EF_Hand_1_Ca_BS.
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.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000313|EMBL:AJE22538.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:AJE22538.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068210};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AJE22538.1}.
FT DOMAIN 3..288
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 316..466
FT /note="Mannose-6-phosphate isomerase type II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01050"
SQ SEQUENCE 481 AA; 53520 MW; FF604A4D189EE01C CRC64;
MIPVILSGGS GSRLWPLSRK QYPKQFLALT SERTLFQQTL QRLAFEGMQS PIVVCNQEHR
FIVKEQLEAV GLHVQGLVLE PFGRNTAPAI ALTAMKLLAE GRDELLLVLP ADHVLADQQA
FEQSLKVAAQ AAEMGEMVLF GIPAHRPETG YGYIKCDLAV QDSLPEGANR VLQFVEKPDL
ARAREFVESG NYFWNSGVFL FRASRFLEEL KEHDPDIYDN CLLTLERSEQ QNDELKVDPA
SFACCPDNSI DYAVMEKTRQ AAAVPLCAGW SDVGCWASIW EVHDKDENGN VTKGDVILHD
THNSLVHGNG KLVTVIGLDN VVVVETKDAT MVVHKDRVQD VKKLVKTLDE QGRPESQNHC
LVYRPWGAYD SVDMGSRFQV KRITVKPGAS LSLQKHHHRA EHWIVVSGTA QVTCDEKTFV
LTENQSTYIP VAAVHRLANP GKIPLEIIEV QSGSYLGEDD IERLEDVYGR TEGVQSRSVA
G
//
