ID A0A0M3TU24_9GAMM Unreviewed; 334 AA.
AC A0A0M3TU24;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000313|EMBL:ALE52185.1};
GN ORFNames=SP60_02395 {ECO:0000313|EMBL:ALE52185.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52185.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52185.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52185.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|ARBA:ARBA00007637}.
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DR EMBL; CP010552; ALE52185.1; -; Genomic_DNA.
DR RefSeq; WP_053951120.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M3TU24; -.
DR STRING; 1705394.SP60_02395; -.
DR KEGG; tho:SP60_02395; -.
DR PATRIC; fig|1705394.5.peg.485; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000058020; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR011912; Heptose_epim.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02197; heptose_epim; 1.
DR PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000058020};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..257
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 334 AA; 37480 MW; ED0BBA7451E4669B CRC64;
MTYSNTDFNN KTILITGGAG FIGSNLAFYF QDNYPDSRVV VFDCFRSEVT FANGNLQSFG
HYKNLIDFTG DVVCGNINSK PDLALLDDYK FDYMFHQAAI SDTRVYDQEI VMQTNVNSFY
DLLNKAKNDD AVMVYASSAA TYGSLPSPQT VGIENPENPY GFSKYMMDQI AYRYSRENPD
MTIVGLKFFN VYGPREYYKA KTSSMVIQLG HQILDGKAPK LFEGSDQILR DFINIEDVIQ
ANIKACNPKQ NGTYNVGTSN PRSFQDIADI LQHELGTDLG TDYIPNPYDG YQMHTQADIS
TTQTNLGFEP VVSLEVGIKA YIPDIKRLHG TDIS
//
