ID A0A1H8V661_9EURY Unreviewed; 330 AA.
AC A0A1H8V661;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN ORFNames=SAMN04487948_11481 {ECO:0000313|EMBL:SEP10960.1};
OS Halogranum amylolyticum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=660520 {ECO:0000313|EMBL:SEP10960.1, ECO:0000313|Proteomes:UP000199126};
RN [1] {ECO:0000313|EMBL:SEP10960.1, ECO:0000313|Proteomes:UP000199126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10121 {ECO:0000313|EMBL:SEP10960.1,
RC ECO:0000313|Proteomes:UP000199126};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000441};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00005812}.
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DR EMBL; FODV01000014; SEP10960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8V661; -.
DR OrthoDB; 145241at2157; -.
DR Proteomes; UP000199126; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR NCBIfam; NF041368; Fbpase2_Halo; 1.
DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 330 AA; 36503 MW; 3C14B54E3045F1B4 CRC64;
MSFHSGTELG AVYDEALEEG FGLVASNIAE PNVMMGLMEG ASQVNSDLLL QLSSGACSFA
GNGDPVAGLK AMGEYIEVIA EQYDVGVFLN MDHQTDMEFI EKQVELDIPS SIMIDASHEP
FEENIETSRQ VVEMINSAGH DILVEAELGR IKGVEDEIVS EKAFYTDPEE AVEFVDQTGC
DLLAISVGTQ HGVAKGQDLE LRPDIARDIR QELRDHGLDT PLVLHGSSGI LPEQLQQLLQ
HGICKVNKDT RYQYEYTRTA FDLYREHTDE LVPPEGVEDD RDGFYNASDW SPNKDHFDPR
VSGRLIRERI AEVYADLAEI SGSAGESRFT
//
