ID A0A0R1Y250_9LACO Unreviewed; 434 AA.
AC A0A0R1Y250;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Altronate oxidoreductase {ECO:0000313|EMBL:KRM33420.1};
GN ORFNames=FC83_GL002811 {ECO:0000313|EMBL:KRM33420.1};
OS Agrilactobacillus composti DSM 18527 = JCM 14202.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Agrilactobacillus.
OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM33420.1, ECO:0000313|Proteomes:UP000051236};
RN [1] {ECO:0000313|EMBL:KRM33420.1, ECO:0000313|Proteomes:UP000051236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM33420.1,
RC ECO:0000313|Proteomes:UP000051236};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
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:KRM33420.1}.
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DR EMBL; AZGA01000052; KRM33420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1Y250; -.
DR STRING; 1423734.FC83_GL002811; -.
DR PATRIC; fig|1423734.3.peg.2858; -.
DR eggNOG; COG0246; Bacteria.
DR Proteomes; UP000051236; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000051236}.
FT DOMAIN 10..130
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 165..403
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 434 AA; 49082 MW; E021132D519A9705 CRC64;
MNKHGLFQGG VAVVQPIDRG MTKMLDEQDD LYTVLLEGKL AGKKVQEHEI VESINETIRP
YEDYQAYLDL AKNDAIQFIF SNTTEAGIAF DPQDTLTARP QNSYPGKLTA LLYERFKLGK
KGFQIIPCEL INHNGNTLKE IVLKYAKLWD LGQNFVDWIN TDNDFYATLV DRIVPGYPKD
RATDLERAWG YHDKLIVKAE PFLIFVIEGN KKLEKLLPLK DAGLNVVVTD DMQPYRNRKV
SLLNGPHTTM SPIARLAGID TVGKVMQDKD FYKFINDEMY QEIIPTVALP KKELVAYAEG
VKERFENPYV NHELSSIALN SISKFKARLL PTFKRYVATN HKLPQRITLA LASYLKIYGG
RADFEPQDTP EVLAAFKTLV QNDDYVTAAL ADAKLWGEDL TQYTGLVTLV KQDLQSLDQG
GARQAVQQIN QKGD
//
