ID Q1YGH0_AURMS Unreviewed; 337 AA.
AC Q1YGH0;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:EAS49255.1};
GN ORFNames=SI859A1_02856 {ECO:0000313|EMBL:EAS49255.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS49255.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS49255.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS49255.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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:EAS49255.1}.
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DR EMBL; AAPJ01000005; EAS49255.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YGH0; -.
DR HOGENOM; CLU_022138_3_2_5; -.
DR BioCyc; AURANTIMONAS:SI859A1_02856-MONOMER; -.
DR Proteomes; UP000000321; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EAS49255.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT DOMAIN 32..299
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 337 AA; 35373 MW; 2D5B18BB8AB5573B CRC64;
MGAVVPAKQE RSGLMVEARH VSTMPARQGT RIEICEVGPR DGFQIEKSFI PTGRKIEIVN
GLIDAGLRKV QVTSFVSPRA VPQLADAAEV LAGVKRRPGT VLTALVPNAR GAERAAETQL
DVMGVFCSAS ETHSRKNVNA SIDETLARFP AVVEIASAAG KRVQGDVATA FGCPFEGDVA
PEQVVRIARF YRDLGIVDLN LGDTTGMATP TNVSALLAAL RAAVPEMTVT LHFHNTRGVG
LANVMVGLAE GVTRYDSSIG GLGGCPFAAG ASGNICTEDL VYLLQESGYE TGIDLDQLID
VARLTQTSLG RELPGQVMKA GPRLTRHGVD DVATAAG
//
