ID K2MI46_BIFBI Unreviewed; 825 AA.
AC K2MI46;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN ORFNames=B217_00020 {ECO:0000313|EMBL:EKF16817.1};
OS Bifidobacterium bifidum IPLA 20015.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1207543 {ECO:0000313|EMBL:EKF16817.1, ECO:0000313|Proteomes:UP000007366};
RN [1] {ECO:0000313|EMBL:EKF16817.1, ECO:0000313|Proteomes:UP000007366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPLA 20015 {ECO:0000313|EMBL:EKF16817.1,
RC ECO:0000313|Proteomes:UP000007366};
RA Gueimonde M., Margolles A., Sanchez B.;
RT "Genome sequence of Bifidobacterium bifidum IPLA 20015.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKF16817.1}.
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DR EMBL; AMPM01000001; EKF16817.1; -; Genomic_DNA.
DR RefSeq; WP_003817358.1; NZ_AMPM01000001.1.
DR AlphaFoldDB; K2MI46; -.
DR PATRIC; fig|1207543.3.peg.3; -.
DR Proteomes; UP000007366; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 17..381
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 605..802
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 825 AA; 92465 MW; 2A8DF06A000F595E CRC64;
MTSPVIGTPW KKLNAPVSEE ALEGVDKYWR VANYLSIGQI YLRSNPLMKE PFTREDVKHR
LVGHWGTTPG LNFLIGHINR FIADHGQNTV FIMGPGHGGP AGTSQSYLDG TYTETYPNIT
KDEAGLQKFF RQFSYPGGIP SHFAPETPGS IHEGGELGYA LSHAYGAIMD NPSLFVPCIV
GDGEAETGPL ATGWQSNKLV NPRTDGIVLP ILHLNGYKIA NPTILSRISD EELHEFFHGM
GYEPYEFVAG FDDEDHMSIH RRFAELFESV WDEICDIKAA ANTDNMHRPF YPMIIFRTPK
GWTCPKYIDG KKTEGSWRAH QVPLASARDT EAHFEVLKNW LESYKPEELF DANGAVKDDV
LAFMPKGELR IGANPNANGG VIRKDLVLPA LEDYEVKEVK EFGHGWGQLE ATRRLGVYTR
DIIKNNMHDF RIFGPDETAS NRLQASYEVT NKQWDAGYIS DEVDEHMHVS GQVVEQLSEH
QMEGFLEAYL LTGRHGIWSS YESFVHVIDS MLNQHAKWLE ATVREIPWRK PIASMNLLVS
SHVWRQDHNG FSHQDPGVTS VLLNKCFHND HVIGIYFATD ANMLLAIAEK CYKSTNKINA
IIAGKQPAAT WLTLDEARAE LAKGAAAWDW ASTAKTNDEA QVVLAAAGDV PTQEIMAASD
KLKALGIKFK VVNVADLLSL QSAKENDEAL TDEEFADIFT ADKPVLFAYH SYAHDVRGLI
YDRPNHDNFN VHGYEEEGST TTPYDMVRVN ELDRYELTAE ALRMIDADKY ADEIQKLEDF
RQEAFQFAVD KGYDHPDYTD WVYSGVKTDK KGAVTATAAT AGDNE
//
