ID A0A268JMI8_9BACI Unreviewed; 487 AA.
AC A0A268JMI8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Altronate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00670};
DE EC=1.1.1.58 {ECO:0000256|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate reductase {ECO:0000256|HAMAP-Rule:MF_00670};
GN Name=uxaB {ECO:0000256|HAMAP-Rule:MF_00670};
GN ORFNames=CHI06_23295 {ECO:0000313|EMBL:PAE35543.1};
OS Bacillus sp. 7884-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021693 {ECO:0000313|EMBL:PAE35543.1, ECO:0000313|Proteomes:UP000216214};
RN [1] {ECO:0000313|EMBL:PAE35543.1, ECO:0000313|Proteomes:UP000216214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7884-1 {ECO:0000313|EMBL:PAE35543.1,
RC ECO:0000313|Proteomes:UP000216214};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH;
CC Xref=Rhea:RHEA:17813, ChEBI:CHEBI:15378, ChEBI:CHEBI:17360,
CC ChEBI:CHEBI:17886, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.58;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00670};
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 -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|HAMAP-Rule:MF_00670}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00670}.
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:PAE35543.1}.
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; NPDD01000213; PAE35543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268JMI8; -.
DR OrthoDB; 9768714at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000216214; Unassembled WGS sequence.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:RHEA.
DR GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00670; Altron_oxidoreduct; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023668; Altronate_OxRdtase.
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 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00670};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00670,
KW ECO:0000313|EMBL:PAE35543.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216214}.
FT DOMAIN 18..172
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 204..458
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
FT BINDING 19..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00670"
SQ SEQUENCE 487 AA; 56090 MW; C9CEB36A043E987C CRC64;
MQRLNNKIYQ EYTSYPEKVL QFGEGNFLRG FIDWQIQVLN EKTDFNGSVV VVQPRGNNKI
ERLNIQDGLF TLYLQGIKEG QLVNQHQVIE SISRGINLFT DYPEYIKLAG TEDLRLIVSN
TTEAGIVFDT TDQLQDRPQK SFPGKLTAFL YHRFIAFAGD ENRGCIIIPC ELIERNGEKL
REIVLQYASL WNLGDEFIEW VENANTFCSS LVDRIVPGFP TDSYKEKIEQ LGYEDELMVV
GEQYHLWVIE GPEWIKNELK VEGTGLNTLI VDDLTPFRIR KVRILNGAHT AMTPVAYLSG
LSTVEESVNN EEIGRFIREM IVEEIVPTLE GPKTELSSFA DDVISRFANP YIKHYLMNIA
LNSISKFQTR NLPALLDYVE KNNSLPKRMV FSLSSMLYFY RGKRGNDVIE LQDDPVNVQF
FKTHWEKFEQ HELTMKELVN VILAEKRLWG MDLTSIPNLD STVCTNLLTI YEMGVKEALK
ELFETSI
//
