ID M5B781_9MICO Unreviewed; 304 AA.
AC M5B781;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Bifunctional folate synthesis protein {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Short=DHNA {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE Includes:
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE EC=2.7.6.3 {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=PPPK {ECO:0000256|RuleBase:RU362079};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000256|RuleBase:RU362079};
DE Short=HPPK {ECO:0000256|RuleBase:RU362079};
GN Name=folBK {ECO:0000313|EMBL:CCE74765.1};
GN ORFNames=CMN_00808 {ECO:0000313|EMBL:CCE74765.1};
OS Clavibacter nebraskensis NCPPB 2581.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE74765.1, ECO:0000313|Proteomes:UP000012170};
RN [1] {ECO:0000313|EMBL:CCE74765.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE74765.1, ECO:0000313|Proteomes:UP000012170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2581 {ECO:0000313|Proteomes:UP000012170};
RA Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA Eichenlaub R., Rueckert C.;
RT "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT nebraskensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000256|RuleBase:RU362079};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC {ECO:0000256|RuleBase:RU362079}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
CC -!- SIMILARITY: Belongs to the DHNA family.
CC {ECO:0000256|RuleBase:RU362079}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00009640}.
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DR EMBL; HE614873; CCE74765.1; -; Genomic_DNA.
DR RefSeq; WP_015489555.1; NC_020891.1.
DR AlphaFoldDB; M5B781; -.
DR KEGG; cmc:CMN_00808; -.
DR PATRIC; fig|1097677.3.peg.686; -.
DR HOGENOM; CLU_023499_2_0_11; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000012170; Chromosome.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00534; DHNA_DHNTPE; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR NCBIfam; TIGR00525; folB; 1.
DR NCBIfam; TIGR00526; folB_dom; 1.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR43071; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR43071:SF1; 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE; 1.
DR Pfam; PF02152; FolB; 1.
DR Pfam; PF01288; HPPK; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCE74765.1};
KW Lyase {ECO:0000256|RuleBase:RU362079};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE74765.1}.
FT DOMAIN 10..122
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 304 AA; 31686 MW; 74C548F7A77A0258 CRC64;
MVTPAPADRI LLTGLRVHAH HGVFAEERRD GQPFVIDLEV ALDLAPAGGS DELGRTLHYG
ELAEEVAAAV GRDPVDLIET VAERVAGVVL AHPVARSVRV TVHKPDAPIA VPFDDVAVVI
ERASALPAPG ETVRAVVAVG SNLGGRRATI ERALASIDEV PGLRVVRTSD LVESVAVTAA
GEDPTKPGYL NGVALVDSGL GPHALLDVLA AIERDLGRVR AERWGDRTID LDVIAYGDAR
IHDERLTVPH PRAAERAFVL GPWLQADPDA ELPGRGRVDA LLAALAPPPA PAAAPAAAAA
EARA
//
