ID H8GLR5_METAL Unreviewed; 652 AA.
AC H8GLR5;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:EIC30592.1};
GN ORFNames=Metal_2911 {ECO:0000313|EMBL:EIC30592.1};
OS Methylomicrobium album BG8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomicrobium.
OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC30592.1, ECO:0000313|Proteomes:UP000005090};
RN [1] {ECO:0000313|EMBL:EIC30592.1, ECO:0000313|Proteomes:UP000005090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG8 {ECO:0000313|EMBL:EIC30592.1,
RC ECO:0000313|Proteomes:UP000005090};
RX PubMed=23580712;
RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA Stein L.Y.;
RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT Methylomicrobium album Strain BG8.";
RL Genome Announc. 1:E0017013-E0017013(2013).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; CM001475; EIC30592.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GLR5; -.
DR STRING; 686340.Metal_2911; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_028734_0_0_6; -.
DR Proteomes; UP000005090; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005090};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 334..507
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 652 AA; 70986 MW; 9E8F996A526F161D CRC64;
MRRDWRLKVN NKNTVILEKT TMAQFPIDLG AYRRVSLAAG NPTLSPDQKA ALKANIQLCR
DAIVFFTATG AARGVGGHTG GPYDTVPEVM ILDALFRGSN GFVPIFFDEA GHRVATQYLM
SVLNGDMPAE KLMLYREAHS HLPGHPELGF TPGVKFSSGR LGHMWPYVNG VAMANPGKTV
FCLGSDGSQQ EGDDAEAARL SVAQGLNVKL LIDDNDVTIA GHPSHYLKGC STAQTLRGHG
VTVFEGDGED LDGLYERIIQ AINTEGPVAV INHRKMCPGI PGIEGSNHGH DVISVKHAIE
YLEARGYTDA IELLKSASPA KQNYTFKGSS DKWDANRNVF GDACVSVLGK MSEADRIAKV
RVIDSDLEGS CGLKKIHDAH PEVFIASGIM ERGNFSAAAG FGMEKGKQGI FGTFSAFLEM
NISEITMARL NHSNVLSHYS HSGIDDMADN TCHFGLNNLF ADNGLDDAYP TNLYFPADPN
QMRACVESVF HDEGLRFIFS TRSKVPLILD ENGNERFGGD YKFVSGKDEV IREGTQGYIV
AFGEALYRAL DAVERLKEEG IDIGLINKPT LNAIDEDMLA KVGKSPLVLV VESFNRKTGL
GSRYGTWLLE RGFTPKFAHL GTHQEGCGGL WEQFPHQGLD PVGIIAKVKS MR
//
