ID E6TL88_MYCSR Unreviewed; 823 AA.
AC E6TL88;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN OrderedLocusNames=Mspyr1_26720 {ECO:0000313|EMBL:ADT99303.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT99303.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT99303.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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}.
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DR EMBL; CP002385; ADT99303.1; -; Genomic_DNA.
DR RefSeq; WP_013471641.1; NC_014814.1.
DR AlphaFoldDB; E6TL88; -.
DR KEGG; msp:Mspyr1_26720; -.
DR HOGENOM; CLU_013954_2_0_11; -.
DR Proteomes; UP000008916; Chromosome.
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 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 12..380
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 597..799
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 823 AA; 91806 MW; 9C73A81EF647BC67 CRC64;
MTTATTAERR PLSDQDVDRL DRWWRAANYL SVGQIYLLDN PLLRTPLTRE DVKPRLLGHW
GTTPGLNFLY AHLNRAIAQR QQSTIYVTGP GHGGPGLVAN AYLDGTYSEI YSDITQDDEG
LRRLFRQFSF PGGIPSHVAP ETPGSIHEGG ELGYALSHAY GAAFDNPDLL VAAVVGDGEA
ETGPLATSWH SNKFVNAAKD GAVLPILHLN GYKIANPTLL ARIPTDELRA LMVGYGHHPY
FFEVPDDEGG PGVDHADAHR RFARLLDDVL DEIADIKTRA REGDESRPAW PMIVFRTPKG
WTGPDYIDGK KTTGSWRAHQ VPLSNARDTK EHLAVLSDWL SSYRPDELFD ADGRLLPEIA
ELAPSGQLRM SDNAHANGGL LLKDLRLPDF REYAVDVPAP GATVAEATRV LGQWLTEVIR
LNPDNFRIFG PDETASNRLQ AVYDATDKQW NAEFFGAEVD EHLARAGRVV EMLSEHQCQG
WLEGYLLTGR HGLFNCYEAF IHIVDSMLNQ HAKWLKVTNH IPWRRPIASL NYLLSSHVWR
QDHNGFSHQD PGFIDHVVNK SAKVVRVYLP PDANTLLSTY DHCLRSRQYV NVVVSGKQPS
PNFLTMEQAV AHCTRGLGIW EWAGSEELGT DPDVVLASAG DIPTLEALAA ADILRQHLPD
LKVRFVNVVD LMRLQDSTEH PHGLPDRDFD MIFTTDRPII FAYHGYPWLI HRLTYRRAGH
DNLHVRGYKE EGTTTTPFDM VMLNDLDRYH LVMDVIDRVP SLGSTCAALR QQMADKRIAA
REYTRAHGED IPEVKDWVWP AARESGFGTA GADGASSTGG DNE
//
