ID V6DNF8_9LACO Unreviewed; 786 AA.
AC V6DNF8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN ORFNames=LSCP400_09801 {ECO:0000313|EMBL:CDK35173.1};
OS Ligilactobacillus salivarius cp400.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1273133 {ECO:0000313|EMBL:CDK35173.1, ECO:0000313|Proteomes:UP000018601};
RN [1] {ECO:0000313|EMBL:CDK35173.1, ECO:0000313|Proteomes:UP000018601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cp400 {ECO:0000313|Proteomes:UP000018601};
RX PubMed=24526652; DOI=10.1128/genomeA.01231-13;
RA Mackenzie D.A., McLay K., Roos S., Walter J., Swarbreck D., Drou N.,
RA Crossman L.C., Juge N.;
RT "Draft Genome Sequence of a Novel Lactobacillus salivarius Strain Isolated
RT from Piglet.";
RL Genome Announc. 2:e01231-e01213(2014).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC ECO:0000256|HAMAP-Rule:MF_01403}.
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:CDK35173.1}.
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DR EMBL; CBVR010000012; CDK35173.1; -; Genomic_DNA.
DR AlphaFoldDB; V6DNF8; -.
DR Proteomes; UP000018601; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02011; TPP_PK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR HAMAP; MF_01403; Phosphoketolase; 1.
DR InterPro; IPR023962; Phosphoketolase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR PANTHER; PTHR31273:SF0; PHOSPHOKETOLASE-RELATED; 1.
DR Pfam; PF03894; XFP; 1.
DR Pfam; PF09363; XFP_C; 1.
DR Pfam; PF09364; XFP_N; 1.
DR PIRSF; PIRSF017245; Phosphoketolase; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 6..366
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 583..782
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 786 AA; 88679 MW; D1B7BEFADD65FE63 CRC64;
MTDYSSQEYL DKLDAYWRAA NYVSVGQLYL KDNPLLRRPL KAEDVKVKPI GHWGTIAGQN
FIYAHLNRVI NKYDLNMFYV EGPGHGGQVM VSNSYLDGSY SEIYPEISQD EQGMKRLFKR
FSFPGGVASH AAPETPGSIH EGGELGYSIS HSVGAVLDNP DLIVAAVVGD GEAETGPLAA
SWQSNKFINP IHDGAVLPIL DLNGFKISNP TILSRESDET LTKYFEGMGW HPIFVEGDDP
KLMHPAMAKA MDEAIEEIKA IQKNARENND PNLPAWPVII FRAPKGWTGP KEWDGEPIEK
SFRAHQIPIP VDQNDMQHAD ALVDWLESYK PEELFDENGK LKAEIAEITP KGDKRMAANP
HTNPGKLIRE VIKPDFRDFA VDTSVPGKEV AQDMTVLGKY LEKVLSDNRH NYRVFGPDET
MSNRLAPIFD VTKRQWLAEI KEPNDQYLAP SGQVIDSQLS EHQAEGFLEG YVLTGRHGFF
ASYESFLRVV DSMLTQHFKW LRKATEQPWR TSIPSLNVIA TSTVFQQDHN GYTHQDPGIL
GHLADKKPEY IREYLPADAN SLLAVFDKTI NDRDKINLIV ASKHPRQQFY SAAEAKELVD
KGLKIIDWAS TDKNAEPDVV IAAAGTEPNL EALAAISILH EKLPDLKIRF INVVDILKLR
SPKVDPRGLS DDEFDAYFTK DKPVIFAFHG YEGLLRDIFY YRHNHNVAFH GYRENGDITT
PFDMRVLSQM DRFDLVKSVA LSLPNADKYG QLVAEMDAKV AKHHQYIRDE GTDLPEVENW
EWKPLD
//