ID H0A2I9_9PROT Unreviewed; 358 AA.
AC H0A2I9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
GN ORFNames=HMPREF9946_03031 {ECO:0000313|EMBL:EHL99687.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL99687.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHL99687.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC {ECO:0000256|ARBA:ARBA00002713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767,
CC ChEBI:CHEBI:57990; EC=4.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001794};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000256|ARBA:ARBA00007389}.
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:EHL99687.1}.
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DR EMBL; AGEZ01000092; EHL99687.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A2I9; -.
DR STRING; 1054213.HMPREF9946_03031; -.
DR PATRIC; fig|1054213.3.peg.2796; -.
DR eggNOG; COG1312; Bacteria.
DR HOGENOM; CLU_058621_0_0_5; -.
DR OrthoDB; 9780250at2; -.
DR BioCyc; ABAC1054213:G1H32-2811-MONOMER; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR Pfam; PF03786; UxuA; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EHL99687.1};
KW Hydrolase {ECO:0000313|EMBL:EHL99687.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nuclease {ECO:0000313|EMBL:EHL99687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292}.
SQ SEQUENCE 358 AA; 38987 MW; E4E52447FBFF3476 CRC64;
MYIGEQLINP TEARLRLSAQ LGAQGIVIDT RPNVQLLDAK GRWDSAKVAE QRKFVERFGL
RLEVMAIDIG SILLDSLYNR KRAAATAEGI RQDIRAAAAG GVTTLKYNVQ MVGITRTGVA
QGRGGVSCSA FNAAEYDPAR DAQFSYWGVG HPDSNREDSD EPVNAIGTPE ACGQVLGDSI
PGVTEEQGWE ALEYFVEQVM PTAEKEGVRL AGHPHDPAYP VGGLNGVNHV VGSLAGIRRF
LDIAPANTSH GLNFCQGTVA EMSDDPNAIV QEAIREFGRR KRIFMVHFRN IKGGYLNFRE
AFPDEGDVDM AESIRSYRSV GYDGILCPDH VPLSDLDPGR ERFFAFALGY TKGLLQAA
//
