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Database: UniProt
Entry: A0A1N7J1B9_9GAMM
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ID   A0A1N7J1B9_9GAMM        Unreviewed;       664 AA.
AC   A0A1N7J1B9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN   ORFNames=SAMN05421760_101468 {ECO:0000313|EMBL:SIS43178.1};
OS   Neptunomonas antarctica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptunomonas.
OX   NCBI_TaxID=619304 {ECO:0000313|EMBL:SIS43178.1, ECO:0000313|Proteomes:UP000185999};
RN   [1] {ECO:0000313|Proteomes:UP000185999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22306 {ECO:0000313|Proteomes:UP000185999};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC       ketose donor to an aldose acceptor, via a covalent intermediate with
CC       the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027,
CC         ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC       metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU004996};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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DR   EMBL; FTOE01000001; SIS43178.1; -; Genomic_DNA.
DR   RefSeq; WP_054342659.1; NZ_LJSI01000053.1.
DR   AlphaFoldDB; A0A1N7J1B9; -.
DR   STRING; 619304.SAMN05421760_101468; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000185999; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU004996};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004996};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          12..32
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   664 AA;  72343 MW;  DC824E39DA5B4FC2 CRC64;
     MSSRRELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WNDFMQHNPS NPQWFDRDRF
     ILSNGHGSML IYSLLHLTGY DVSIDDIKNF RQLHSKTAGH PEYGYCPGVE TTTGPLGQGL
     TNAVGFALAE KILAAQFNRE GHEIIDHNTY VFMGDGCMME GISHEACSLA GTLGLGKLVA
     FWDDNGISID GEVEGWYTDD NVKRFEAYGW QVIPGVDGHD ADQIRDAIVK ARENTERPTL
     ICCKTTIGFG SPNKEGKEDC HGAPLGEAEI ALTRERLNWP HPAFEIPEDL YADWNAKQAG
     THAENEWDER FVAYRAEFPE LASELLRRMS GDLPADFSDK ADAWIADVAA KGETIASRKA
     SQNALNAYGP LLPELLGGSA DLAGSNLTIW SGAKGINKDD ASGNYLYYGV REFGMSAIMN
     GLALHGGFIP YGATFLVFME YARNALRMAA LMKQRVIHVY THDSIGLGED GPTHQPVEQV
     SNLRHTPNMS CWRPGDAVES AVAWKAALER TDGPTALVFS RQNLPHQQRT PEQIANIARG
     GYILRDTDGQ PDAILIATGS ELGLVMDAAA VLTAEGKQIR VVSMPETGVF DRQDAAYRES
     VLPAAVTARV AVEALQADFW YKYVGLNGAI VGMTTFGESA PASDLFKHFG FTVDNVVANV
     KSLL
//
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