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Database: UniProt
Entry: N9N7N1_9GAMM
LinkDB: N9N7N1_9GAMM
Original site: N9N7N1_9GAMM 
ID   N9N7N1_9GAMM            Unreviewed;       371 AA.
AC   N9N7N1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836, ECO:0000256|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153, ECO:0000256|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   ORFNames=F894_00131 {ECO:0000313|EMBL:ENX16999.1};
OS   Acinetobacter sp. CIP 51.11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144670 {ECO:0000313|EMBL:ENX16999.1, ECO:0000313|Proteomes:UP000018464};
RN   [1] {ECO:0000313|EMBL:ENX16999.1, ECO:0000313|Proteomes:UP000018464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 51.11 {ECO:0000313|EMBL:ENX16999.1,
RC   ECO:0000313|Proteomes:UP000018464};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 51.11.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate +
CC         formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830;
CC         EC=4.1.99.12; Evidence={ECO:0000256|ARBA:ARBA00000141,
CC         ECO:0000256|HAMAP-Rule:MF_00180};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_00180};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004904, ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00180}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000256|ARBA:ARBA00008976}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000256|ARBA:ARBA00005520}.
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:ENX16999.1}.
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DR   EMBL; APRU01000003; ENX16999.1; -; Genomic_DNA.
DR   RefSeq; WP_005245353.1; NZ_KB850128.1.
DR   AlphaFoldDB; N9N7N1; -.
DR   PATRIC; fig|1144670.3.peg.116; -.
DR   HOGENOM; CLU_020273_1_2_6; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000018464; Unassembled WGS sequence.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR036144; RibA-like_sf.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF34; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   PIRSF; PIRSF001259; RibA; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00180};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_00180}.
FT   DOMAIN          208..365
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   BINDING         27..28
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         32
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         140..144
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            126
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            164
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   371 AA;  40702 MW;  DC220B1C71DC8E04 CRC64;
     MPLNTVEELV ADIRAGKMVI LMDDEDRENE GDLVIAATHV RPEDINFMIT HARGLVCLTL
     SKERCQQLNL PLMVDANGAQ HGTNFTLSIE AAEGISTGIS PAERAHTIQT AVAAHAKPAD
     IVQPGHIFPL MAQPGGVLHR AGHTEAGCDL SRLAGLEPAS VICEIINEDG TMARRPDLEV
     FAEKHGLKIG TIADLIHYRM TNEQTVERID QQSIDTEYGS FDLYRYRELG NPDIHLALVK
     GEPKDGVTTV RVHGFNPTRD LLKLKKQDGE PAWNLDRALK EISNSDRGVL VWIGQHHLQD
     LGPALDNLKA PKNVKSNSAL SQQYQTIGVG AQILRDLGVE KMKLLSSPLR FNALSGFNLE
     VVEYITAQQT S
//
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