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Database: UniProt
Entry: A0A154BPP5_ANASB
LinkDB: A0A154BPP5_ANASB
Original site: A0A154BPP5_ANASB 
ID   A0A154BPP5_ANASB        Unreviewed;       311 AA.
AC   A0A154BPP5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:KYZ75912.1};
GN   ORFNames=AXX12_10640 {ECO:0000313|EMBL:KYZ75912.1};
OS   Anaerosporomusa subterranea.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Anaerosporomusa.
OX   NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ75912.1, ECO:0000313|Proteomes:UP000076268};
RN   [1] {ECO:0000313|EMBL:KYZ75912.1, ECO:0000313|Proteomes:UP000076268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU4 {ECO:0000313|EMBL:KYZ75912.1,
RC   ECO:0000313|Proteomes:UP000076268};
RA   Choi J.K., Shah M., Yee N.;
RT   "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT   anaerobe isolated from saprolite.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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:KYZ75912.1}.
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DR   EMBL; LSGP01000020; KYZ75912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A154BPP5; -.
DR   STRING; 1794912.AXX12_10640; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000076268; Unassembled WGS sequence.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
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; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KYZ75912.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076268};
KW   Transferase {ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          6..273
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   311 AA;  33502 MW;  F56E6223AFEC8D08 CRC64;
     MWPSKVTICE VGLRDGLQNE KKILSVEEKL QLLDMAVDSG VRIIEIGSFV HPKAVPQMAD
     TDQVVQKMQK VDGVEYRALV ANLKGVERAH AAGLSKVKLT VSASEAHCIN NFNKTPVEMI
     EGFASCMEFI SKNNMEVSGA ISTSFGCPFQ GKVPVEQVEN AVRGFLKLGI TELSLSDTTG
     MANPRQVYEL GSYMVKAFPQ VQWVLHFHNT RDMALANIAA GIEAGVRTFD GAFAGLGGCP
     FAPGASGNVA TEDVVHMLHE MGIDTGINLL KAMDTARMAA KLVGHEAASA VLKAGRCEDI
     TKEKVQHQSN K
//
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