HOA1_MYCA9
ID HOA1_MYCA9 Reviewed; 359 AA.
AC B1MH40;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=MAB_0626;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM60724.1; -; Genomic_DNA.
DR AlphaFoldDB; B1MH40; -.
DR SMR; B1MH40; -.
DR EnsemblBacteria; CAM60724; CAM60724; MAB_0626.
DR KEGG; mab:MAB_0626; -.
DR OMA; DLYKMMD; -.
DR Proteomes; UP000007137; Chromosome.
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..359
FT /note="4-hydroxy-2-oxovalerate aldolase 1"
FT /id="PRO_0000387844"
FT DOMAIN 23..275
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 31..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 32
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 31
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 359 AA; 37778 MW; 7416A8E15DB6C6C5 CRC64;
MGSDTSTQLL GTDGIFFDAA WDVRVTDTSL RDGSHHKRHQ FTADEVRAIV AALDGAGVPV
IEVTHGDGLG GSSFNYGFSK TPEQELIKLA AQTATNAKIA FLMLPGVGTK EDIIEAQGNG
GSICRIATHC TEADVSIQHF GLARERGLET VGFLMMSHTI SPEKLAKQAR IMADAGCQCV
YVVDSAGALV LDGVADRVAA VVAELGSDAQ VGFHGHENLG LGVANSIEAV RAGAKQIDGS
TRRFGAGAGN APVEALIGVF DKIGVKTGID FFDIADAAEE VVAPAMPAEC LLDRNALIMG
YSGVYSSFLK HAIRQGERYG VPAHQLLHRA GERKLIGGQE DQLIDIALEI QRENAANGQ