HOA1_NOVAD
ID HOA1_NOVAD Reviewed; 346 AA.
AC A4XF35;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA 1 {ECO:0000255|HAMAP-Rule:MF_01656};
DE EC=4.1.3.39 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase 1 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_01656};
GN OrderedLocusNames=Saro_3687;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL2.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate;
CC Xref=Rhea:RHEA:22624, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:73143; EC=4.1.3.39; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01656};
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR EMBL; CP000677; ABP64546.1; -; Genomic_DNA.
DR RefSeq; WP_011906930.1; NC_009427.1.
DR AlphaFoldDB; A4XF35; -.
DR SMR; A4XF35; -.
DR STRING; 279238.Saro_3687; -.
DR EnsemblBacteria; ABP64546; ABP64546; Saro_3687.
DR KEGG; nar:Saro_3687; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_5; -.
DR OMA; WARENGM; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000009134; Plasmid pNL2.
DR GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07943; DRE_TIM_HOA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01656; HOA; 1.
DR InterPro; IPR017629; 4OH_2_O-val_aldolase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012425; DmpG_comm.
DR InterPro; IPR035685; DRE_TIM_HOA.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF07836; DmpG_comm; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR03217; 4OH_2_O_val_ald; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Lyase; Manganese; Metal-binding; Plasmid;
KW Reference proteome.
FT CHAIN 1..346
FT /note="4-hydroxy-2-oxovalerate aldolase 1"
FT /id="PRO_0000387875"
FT DOMAIN 13..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 204
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 346 AA; 37326 MW; 2724E8329BA57375 CRC64;
MTSNFNVEAG DKLYIQDVTL RDGMHAVRHM YGIDHVRSIA SALDKAGVDA IEVAHGDGLS
GASFNYGFGA HTDWEWLEAV ADVLEKSVLT TLILPGVGTV EELRRAYDIG VRSVRVATHC
TEADVSKQHI GIARDLGMDV SGFLMMSHMI EPEALAQQAS LMESYGAQCV YVTDSGGALD
MDGVKARLEA YDRVLKPETQ RGIHAHHNLA LGVANSIVAA QCGAVRIDAS LTGMGAGAGN
APLEVFIAAA DRKGWNHGCD VMMLMDAAED LVRPLQDRPV RVDRETLALG YAGVYSSFLR
HAEKAAETYG LDTRTILVEL GRRKMVGGQE DMIVDVALDM LKEQQA
