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Database: UniProt
Entry: N9G4C0_ACILW
LinkDB: N9G4C0_ACILW
Original site: N9G4C0_ACILW 
ID   N9G4C0_ACILW            Unreviewed;       325 AA.
AC   N9G4C0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU004155};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU004155};
GN   ORFNames=F924_00662 {ECO:0000313|EMBL:ENW29858.1};
OS   Acinetobacter lwoffii ATCC 9957 = CIP 70.31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1311804 {ECO:0000313|EMBL:ENW29858.1, ECO:0000313|Proteomes:UP000013033};
RN   [1] {ECO:0000313|EMBL:ENW29858.1, ECO:0000313|Proteomes:UP000013033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 70.31 {ECO:0000313|EMBL:ENW29858.1,
RC   ECO:0000313|Proteomes:UP000013033};
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 lwoffii CIP 70.31.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
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|ARBA:ARBA00001469,
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,
CC       ECO:0000256|RuleBase:RU004155}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012, 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:ENW29858.1}.
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DR   EMBL; APQT01000021; ENW29858.1; -; Genomic_DNA.
DR   RefSeq; WP_004645437.1; NZ_KB849829.1.
DR   AlphaFoldDB; N9G4C0; -.
DR   PATRIC; fig|1217667.3.peg.626; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000013033; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW   ECO:0000256|RuleBase:RU004155};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW   Transferase {ECO:0000256|RuleBase:RU004155}.
SQ   SEQUENCE   325 AA;  35490 MW;  DD7D2989DC36C761 CRC64;
     MTLTALNQLK NLTTIVADSS DLSAIEKFRP LDATTNPSLI TAAAKQPENQ ALIEAAFQQA
     QQEGYADDAL IERTIDILTV KFGVEILKLI EGRVSTEVDA SLSFNTEATI AKAKELLALY
     AQYGIDSDRI LIKIASTWEG IQAAKALEEQ GIHTNLTLLF GQHQAHACAD AKVTLISPFV
     GRILDWYKKA EGVESYPIEK DPGVLSVKRI YEFYKAHGIQ TEIMGASFRS IDQVLGLSGC
     DLLTVAPNLL AELENDQREV QAQLSAKDIK VQGELSPISP ADFEAQLKQD PMASELLQGG
     IDGFIKAREQ LAALLRETFL STTEI
//
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