ID A0A1Z9JH11_9CYAN Unreviewed; 390 AA.
AC A0A1Z9JH11;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN ORFNames=CBD37_02260 {ECO:0000313|EMBL:OUW30007.1};
OS Cyanobacteria bacterium TMED177.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1986677 {ECO:0000313|EMBL:OUW30007.1, ECO:0000313|Proteomes:UP000195337};
RN [1] {ECO:0000313|EMBL:OUW30007.1, ECO:0000313|Proteomes:UP000195337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED177 {ECO:0000313|EMBL:OUW30007.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC step 2/3. {ECO:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC Rule:MF_00492, ECO:0000256|RuleBase:RU004155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155}.
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:OUW30007.1}.
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DR EMBL; NHIA01000018; OUW30007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9JH11; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000195337; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR HAMAP; MF_00492; Transaldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00874; talAB; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00492};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00492}.
FT DOMAIN 352..387
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 135
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ SEQUENCE 390 AA; 42630 MW; 644E3A222ABCD321 CRC64;
MATLLDQLSE MTVVVADTGD LEAIRKFTPR DATTNPSLIL AAAQIPAYQN LIDEALRSSR
KLIGDDAPVE DVVLEALDEI SVIFGKEILK IVPGRVSTEV DARLSFNTDA TIEKGRKLIR
LYNDAGISND RVLIKIASTW EGIKAAEVLE KEGIHCNLTL LFGFGQAVAC AEAGVTLISP
FVGRILDWYK ADTGRDSYPG PEDPGVISVT RIFNYFKTFG YGTEVMGASF RNLDEITELA
GCDLLTISPK LLDQLRDSDA TLVRKLDAAN PIGGETQIHV DRESFDAMMK EDRMATDKLG
EGIKGFSKAI ETLERQLGHR LAELEGGEAF RHAVQEIFML NDMNGDGCIT RDEWLGSDAV
FDALDQDHDG RLTPDEVRKG FGAALTLTTA
//
