HOA2_AZOSB
ID HOA2_AZOSB Reviewed; 342 AA.
AC A1K6Y4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
GN Name=mhpE; OrderedLocusNames=azo1972;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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}.
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; AM406670; CAL94589.1; -; Genomic_DNA.
DR RefSeq; WP_011765705.1; NC_008702.1.
DR AlphaFoldDB; A1K6Y4; -.
DR SMR; A1K6Y4; -.
DR STRING; 62928.azo1972; -.
DR EnsemblBacteria; CAL94589; CAL94589; azo1972.
DR KEGG; azo:azo1972; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_4; -.
DR OMA; YVGGQED; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000002588; 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;
KW Reference proteome.
FT CHAIN 1..342
FT /note="4-hydroxy-2-oxovalerate aldolase 2"
FT /id="PRO_0000387781"
FT DOMAIN 8..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 16..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 17
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 342 AA; 36453 MW; 4C507BC65EB5E8DB CRC64;
MDLRGTRITV HDMTLRDGMH PKRHLMTLEQ MKTIAQGLDQ AGIPLIEVTH GDGLGGSSVN
YGFPAHTDEE YLGAVIPLMK QAKVSALLLP GIGTVDHLKM AHELGVNTIR VATHCTEADV
SEQHISYARK LGMDTVGFLM MAHMNSPEGL VQQAKLMESY GANCIYVTDS AGHLLPDTVK
ARISAVRDAL KPETELGFHG HHNLAMGVAN SIAAIEAGAT RIDAAAAGLG AGAGNTPMEV
LIAVCDLMGI ETGVDVFKIQ DVAEDLVVPI MDFPIRIDRD ALTLGYAGVY GSFLLFAKRA
EKKYGVPARE ILVEMGRRGM VGGQEDMIED TAITLAKASA AA