ID A0A1M5RVR5_9RHOB Unreviewed; 276 AA.
AC A0A1M5RVR5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Fructose-bisphosphate aldolase, class II {ECO:0000313|EMBL:SHH30336.1};
GN ORFNames=SAMN05444003_2721 {ECO:0000313|EMBL:SHH30336.1};
OS Cognatiyoonia sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHH30336.1, ECO:0000313|Proteomes:UP000184074};
RN [1] {ECO:0000313|EMBL:SHH30336.1, ECO:0000313|Proteomes:UP000184074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28715 {ECO:0000313|EMBL:SHH30336.1,
RC ECO:0000313|Proteomes:UP000184074};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000256|ARBA:ARBA00005215}.
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DR EMBL; FQXB01000005; SHH30336.1; -; Genomic_DNA.
DR RefSeq; WP_072901975.1; NZ_FQXB01000005.1.
DR AlphaFoldDB; A0A1M5RVR5; -.
DR STRING; 1508389.SAMN05444003_2721; -.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000184074; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000184074};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
SQ SEQUENCE 276 AA; 29363 MW; 8C1AB61A5B7D7AD8 CRC64;
MPLVTLKDVL QPALKNGYAV GGLVTLGWEE MRAYVAAAEA ENCPVILQAG PSCREHTPLP
ILGKMFRQLA EAASVPVVAH LDHGYTLVEC KEALESGFTS LMFDGSRKPL SQNIDETAQI
AEMAHSAGIS CEGEIGFVGY DNGEASAGTD PQEAAKFATE SGVDAMAISV GNVHLQQDQS
GGLDEERIAA IQAVTEIPLV IHGGSGVPAE QRRRLAQTTN ICKFNIGTEL RMAFGEALRE
AVNADPKRFD RVSILKETHD PVVTAARTVL ANLKGN
//
