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Database: UniProt
Entry: A0A0B8ZZR0_9SPHN
LinkDB: A0A0B8ZZR0_9SPHN
Original site: A0A0B8ZZR0_9SPHN 
ID   A0A0B8ZZR0_9SPHN        Unreviewed;       343 AA.
AC   A0A0B8ZZR0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE            Short=HOA {ECO:0000256|HAMAP-Rule:MF_01656};
DE            EC=4.1.3.39 {ECO:0000256|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
GN   ORFNames=NJ75_03643 {ECO:0000313|EMBL:KHS43824.1};
OS   Novosphingobium subterraneum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS43824.1, ECO:0000313|Proteomes:UP000031338};
RN   [1] {ECO:0000313|EMBL:KHS43824.1, ECO:0000313|Proteomes:UP000031338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS43824.1,
RC   ECO:0000313|Proteomes:UP000031338};
RA   Gan H.M., Gan H.Y., Savka M.A.;
RT   "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL   Submitted (OCT-2014) 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:0000256|HAMAP-
CC         Rule:MF_01656};
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC       {ECO:0000256|ARBA:ARBA00008944, ECO:0000256|HAMAP-Rule:MF_01656}.
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:KHS43824.1}.
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DR   EMBL; JRVC01000021; KHS43824.1; -; Genomic_DNA.
DR   RefSeq; WP_039336977.1; NZ_JRVC01000021.1.
DR   AlphaFoldDB; A0A0B8ZZR0; -.
DR   STRING; 48936.NJ75_03643; -.
DR   PATRIC; fig|48936.3.peg.3675; -.
DR   Proteomes; UP000031338; Unassembled WGS sequence.
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; 1.10.8.60; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR03217; 4OH_2_O_val_ald; 1.
DR   PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR   Pfam; PF07836; DmpG_comm; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|HAMAP-Rule:MF_01656};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01656};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01656};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01656}.
FT   DOMAIN          10..262
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         18..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         19
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   343 AA;  36994 MW;  D681BCEC3A1F239E CRC64;
     MTFNPESDRL YIQDVTLRDG MHAILHMYGT DSVRTIAKAL DDAGVDAIEV SHGDGLNGST
     FNYGFGAHTD WDWIEAAADV IKNAVLTTLL VPGIGTAEEL KRAYSMGVRS VRVATHCTEA
     DVGKQHIGIA RDLGMDVSGF LMMSHMIEPE ALAQQALLME SYGAQCVYVT DSGGALDMDG
     VTARLQAYDR VLKPETQRGI HAHHNLSLGV ANSIVAAQAG AVRIDASLAG MGAGAGNAPL
     EVFIAAANRK GWKHRCDVMA LMDAADDIIR PLQDRPVRVD RETLSLGYAG VYSSFLRHAE
     KASEQYGIDT REILVELGNR RMVGGQEDMI IDVALDLIKA RAN
//
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