OTNC_HAEIN
ID OTNC_HAEIN Reviewed; 210 AA.
AC Q57199; O05040;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=3-oxo-tetronate 4-phosphate decarboxylase {ECO:0000303|PubMed:27402745};
DE EC=4.1.1.104 {ECO:0000269|PubMed:27402745};
GN Name=otnC {ECO:0000303|PubMed:27402745}; OrderedLocusNames=HI_1012;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=27402745; DOI=10.1073/pnas.1605546113;
RA Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S.,
RA Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V.,
RA Jacobson M.P., Almo S.C., Gerlt J.A.;
RT "Assignment of function to a domain of unknown function: DUF1537 is a new
RT kinase family in catabolic pathways for acid sugars.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016).
CC -!- FUNCTION: Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate
CC to dihydroxyacetone phosphate (DHAP) and CO(2).
CC {ECO:0000269|PubMed:27402745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-4-O-phospho-D-erythronate + H(+) = CO2 +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:52416, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57642, ChEBI:CHEBI:136593;
CC EC=4.1.1.104; Evidence={ECO:0000269|PubMed:27402745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-4-O-phospho-L-erythronate + H(+) = CO2 +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:52404, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57642, ChEBI:CHEBI:136592;
CC EC=4.1.1.104; Evidence={ECO:0000269|PubMed:27402745};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0AB87};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0AB87};
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000305}.
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; L42023; AAC22673.1; -; Genomic_DNA.
DR PIR; B64108; B64108.
DR RefSeq; NP_439173.1; NC_000907.1.
DR RefSeq; WP_005647883.1; NC_000907.1.
DR AlphaFoldDB; Q57199; -.
DR SMR; Q57199; -.
DR STRING; 71421.HI_1012; -.
DR EnsemblBacteria; AAC22673; AAC22673; HI_1012.
DR KEGG; hin:HI_1012; -.
DR PATRIC; fig|71421.8.peg.1056; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_2_6; -.
DR OMA; ICRYGRS; -.
DR PhylomeDB; Q57199; -.
DR BioCyc; HINF71421:G1GJ1-1052-MON; -.
DR BioCyc; MetaCyc:MON-20188; -.
DR BRENDA; 4.1.1.104; 2529.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..210
FT /note="3-oxo-tetronate 4-phosphate decarboxylase"
FT /id="PRO_0000162931"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ SEQUENCE 210 AA; 23243 MW; 4800CA987DBDF01F CRC64;
MTDLAQKELM VQLGRSFYER GYTVGGAGNL SVRLDDNRVL VTPTGSSLGR LSVERLSVLD
MEGNLLGGDK PSKEAVFHLA MYKKNPECKA IVHLHSTYLT ALSCLDNLDP NNAIEPFTPY
YVMRVGKMQV IPYYRPGSPK IAEELSNRAL TGKAFLLANH GVVVTGSDLL DAADNTEELE
ETAKLFFTLQ GQKIRYLTDT EVKDLENRGK
