ID R6CA60_9CLOT Unreviewed; 194 AA.
AC R6CA60;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Dipicolinate synthase subunit B {ECO:0000256|PIRNR:PIRNR001390};
DE Short=DPA synthase subunit B {ECO:0000256|PIRNR:PIRNR001390};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR001390};
DE AltName: Full=Spore dipicolinate synthase subunit B {ECO:0000256|PIRNR:PIRNR001390};
DE AltName: Full=Stage V sporulation protein FB {ECO:0000256|PIRNR:PIRNR001390};
GN ORFNames=BN513_01898 {ECO:0000313|EMBL:CDA62227.1};
OS Clostridium sp. CAG:169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262778 {ECO:0000313|EMBL:CDA62227.1, ECO:0000313|Proteomes:UP000018302};
RN [1] {ECO:0000313|EMBL:CDA62227.1, ECO:0000313|Proteomes:UP000018302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:169 {ECO:0000313|Proteomes:UP000018302};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with DpaA, catalyzes the conversion of
CC dihydrodipicolinate to dipicolinate (DPA).
CC {ECO:0000256|PIRNR:PIRNR001390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-dihydrodipicolinate + NADP(+) = dipicolinate + H(+) +
CC NADPH; Xref=Rhea:RHEA:47092, ChEBI:CHEBI:15378, ChEBI:CHEBI:30620,
CC ChEBI:CHEBI:36167, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|PIRNR:PIRNR001390};
CC -!- SUBUNIT: Dipicolinate synthase likely consists of DpaA and DpaB, since
CC both proteins are required for DPA synthesis.
CC {ECO:0000256|PIRNR:PIRNR001390}.
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:CDA62227.1}.
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DR EMBL; CBCF010000215; CDA62227.1; -; Genomic_DNA.
DR AlphaFoldDB; R6CA60; -.
DR STRING; 1262778.BN513_01898; -.
DR Proteomes; UP000018302; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR InterPro; IPR014214; Dipicolinic_acid_synth_B.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR NCBIfam; TIGR02852; spore_dpaB; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR PIRSF; PIRSF001390; Dipicolinate_synth_subunit_B; 1.
DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|PIRNR:PIRNR001390};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR001390};
KW Reference proteome {ECO:0000313|Proteomes:UP000018302};
KW Sporulation {ECO:0000256|PIRNR:PIRNR001390}.
FT DOMAIN 8..159
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
SQ SEQUENCE 194 AA; 21352 MW; 44EEB952F3F7F04A CRC64;
MNEHAPVRVG FAMTGSFCTF SQVIDQMEQM AQQTGWQLYP ILSPNAYETD TRFGSAQQFR
RRIEEICGRE IWHTLTQTEP IGPKKLLDVL LVAPCTGNTL GKLANGITDT SVTLAVKAHL
RNARPVVLAV STNDALANAG KNIGSLLNSK NIYFVPMRQD APEQKPCSIV ADFSRLTDTV
QSALSARQLQ PLFC
//
