ID   HOA_STRTE               Reviewed;         357 AA.
AC   Q9X9Q0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE            Short=HOA {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 {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN   Name=nikb {ECO:0000303|PubMed:10503541};
OS   Streptomyces tendae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Tue901;
RX   PubMed=10503541; DOI=10.1007/pl00008637;
RA   Bruntner C., Lauer B., Schwarz W., Mohrle V., Bormann C.;
RT   "Molecular characterization of co-transcribed genes from Streptomyces
RT   tendae Tu901 involved in the biosynthesis of the peptidyl moiety of the
RT   peptidyl nucleoside antibiotic nikkomycin.";
RL   Mol. Gen. Genet. 262:102-114(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of the peptidyl nucleoside
CC       antibiotic nikkomycin. {ECO:0000269|PubMed:10503541}.
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; Y18574; CAB46532.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X9Q0; -.
DR   SMR; Q9X9Q0; -.
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.
FT   CHAIN           1..357
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387926"
FT   DOMAIN          15..265
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        27
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         23..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         24
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         177
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   SITE            23
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   357 AA;  37146 MW;  0B44372DB99234F8 CRC64;
     MSQEAARDAA AGRPVQIHDP TLRDGQHAVR HSLGAEQFRA YLKAADAAAV PVVEVGHGNG
     LAASSLQVGR ARLSDDEMMS IARETLTTSK LGVLMFPGWA TTQDIKNALA YEVDLVRIAT
     HCTEASVAER HLGFLRDEGV EAHGMVVMTH MASPDQLAEE CARLVGYGAT GVGILDSSGH
     FLPSDVTARI GAICAAVDVP VMFHGHNNLG MAVANSIAAA QAGAGILDAC ARGFGAGAGN
     TQLEVLVPVL ERLGFRTGID LYRLLDAADI AGRELMPAPP TIDSVSIVSG LAGVFSGFKK
     PVLDIAAREG VDPRDIFFEL GRRQVVAGQE DLIVEVALAL RAARDGASPA SSGTGPC