ID A0A0S9DB27_9MICC Unreviewed; 794 AA.
AC A0A0S9DB27;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN ORFNames=ASF21_01910 {ECO:0000313|EMBL:KQO03111.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO03111.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQO03111.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLU01000001; KQO03111.1; -; Genomic_DNA.
DR RefSeq; WP_055766036.1; NZ_LMLU01000001.1.
DR AlphaFoldDB; A0A0S9DB27; -.
DR STRING; 1736303.ASF21_01910; -.
DR Proteomes; UP000053418; 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 5..368
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 583..784
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 794 AA; 87829 MW; 0E60E3AD7C8AD0C0 CRC64;
MAHLDIDGLD AWWRAANYVS VGQIYLRDNA LLTRPLVGED VKARLLGHWG TTPGLNFVYA
HLNRVIAERR QEMLFVTGPG HGGPANVANA WLEGTYSEIY SNIGSDGAGL NALFKQFSYP
GGIPSHAAPE TPGSIHEGGE LGYSLAHAYG AVFDNPSLIA AAVVGDGEAE TGPLATSWHS
TSFVDPAVDG AVLPILHLNG YKIANPTVLA RMPEEQLRQL MYGYGYDPHF VTVSDPRATE
AAHRDFAAVL DTCIDEIHDI QARARTSPAG GGAGAARWPM IVLRSPKGWT GPAEVDGKPV
EGTWRAHQVP LSEIHDNEEH LHQLEEWLRS YDPGSLFTDE GGLRPEIARL APDGDLRMSA
TPYANGGRLL RDLVLPAYAE HAVEVAHPGS EKVSPMITAG GYLRDIIERN PHNFRLFGPD
ETASNRLSAV YEVTDKVWQP RIEDVDEHLA RSGRVMEVLS EHLCQGWLEG YLLTGRHGVF
SCYEAFVHIV DSMFNQYAKW LEIHRKLPWR QPIASFTYML SSHVWQQDHN GFSHQDPGFI
DHVVNKKADV IRVYLPPDAN TMLAVTDHCL QARDTINVIV TGKQPTPTWF GPEEARLHVT
RGIGVLDFAG SEESGVEPDV VLGCAGDVPT LEVIAAAGLL TAGIPGLKIR VVNVVDLMRL
QDSTEHPHGL SAREFDTLFT TSKPVIFAYH GYPWLIHRLT YRRNNHPNLH VRGYKEEGTT
TTPFDMAMLN QIDRFQLAMD VIDRVPTLGA TEARFRQDLQ DQRQRAWQYT RDAGKDLESI
TGWTLDESSP DDAK
//
