HMGCL_BACSU
ID HMGCL_BACSU Reviewed; 299 AA.
AC O34873; Q799L7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Hydroxymethylglutaryl-CoA lyase YngG;
DE Short=HL;
DE Short=HMG-CoA lyase;
DE EC=4.1.3.4;
DE AltName: Full=3-hydroxy-3-methylglutarate-CoA lyase;
GN Name=yngG; OrderedLocusNames=BSU18230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387222; DOI=10.1099/00221287-143-11-3443;
RA Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.;
RT "Sequence completion, identification and definition of the fengycin operon
RT in Bacillus subtilis 168.";
RL Microbiology 143:3443-3450(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS), AND SUBUNIT.
RX PubMed=16330546; DOI=10.1074/jbc.m507996200;
RA Forouhar F., Hussain M., Farid R., Benach J., Abashidze M., Edstrom W.C.,
RA Vorobiev S.M., Xiao R., Acton T.B., Fu Z., Kim J.-J.P., Miziorko H.M.,
RA Montelione G.T., Hunt J.F.;
RT "Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases
RT suggest a common catalytic mechanism among a family of TIM barrel
RT metalloenzymes cleaving carbon-carbon bonds.";
RL J. Biol. Chem. 281:7533-7545(2006).
CC -!- FUNCTION: Involved in the catabolism of branched amino acids such as
CC leucine. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:16330546}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR EMBL; Y13917; CAA74217.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13706.1; -; Genomic_DNA.
DR PIR; D69893; D69893.
DR RefSeq; NP_389705.1; NC_000964.3.
DR RefSeq; WP_003231525.1; NZ_JNCM01000035.1.
DR PDB; 1YDO; X-ray; 2.71 A; A/B/C/D=1-299.
DR PDBsum; 1YDO; -.
DR AlphaFoldDB; O34873; -.
DR SMR; O34873; -.
DR STRING; 224308.BSU18230; -.
DR PaxDb; O34873; -.
DR PRIDE; O34873; -.
DR EnsemblBacteria; CAB13706; CAB13706; BSU_18230.
DR GeneID; 939515; -.
DR KEGG; bsu:BSU18230; -.
DR PATRIC; fig|224308.179.peg.1988; -.
DR eggNOG; COG0119; Bacteria.
DR InParanoid; O34873; -.
DR OMA; FGGCPMA; -.
DR PhylomeDB; O34873; -.
DR BioCyc; BSUB:BSU18230-MON; -.
DR BRENDA; 4.1.3.4; 658.
DR UniPathway; UPA00896; UER00863.
DR EvolutionaryTrace; O34873; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; PTHR42738; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..299
FT /note="Hydroxymethylglutaryl-CoA lyase YngG"
FT /id="PRO_0000360168"
FT DOMAIN 7..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 240
FT /evidence="ECO:0000305"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:1YDO"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1YDO"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1YDO"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1YDO"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:1YDO"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:1YDO"
SQ SEQUENCE 299 AA; 32644 MW; 64F7C1C9F4F49DAC CRC64;
MPYPKKVTIK EVGPRDGLQN EPVWIATEDK ITWINQLSRT GLSYIEITSF VHPKWIPALR
DAIDVAKGID REKGVTYAAL VPNQRGLENA LEGGINEACV FMSASETHNR KNINKSTSES
LHILKQVNND AQKANLTTRA YLSTVFGCPY EKDVPIEQVI RLSEALFEFG ISELSLGDTI
GAANPAQVET VLEALLARFP ANQIALHFHD TRGTALANMV TALQMGITVF DGSAGGLGGC
PYAPGSSGNA ATEDIVYMLE QMDIKTNVKL EKLLSAAKWI EEKMGKPLPS RNLQVFKSS
