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ACSM3_PONAB
ID   ACSM3_PONAB             Reviewed;         586 AA.
AC   Q5REV5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Acyl-coenzyme A synthetase ACSM3, mitochondrial;
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:Q3UNX5};
DE   AltName: Full=Acyl-CoA synthetase medium-chain family member 3;
DE   AltName: Full=Butyrate--CoA ligase 3;
DE   AltName: Full=Butyryl-coenzyme A synthetase 3;
DE   AltName: Full=Middle-chain acyl-CoA synthetase 3;
DE   AltName: Full=Propionate--CoA ligase;
DE            EC=6.2.1.17 {ECO:0000250|UniProtKB:Q3UNX5};
DE   AltName: Full=Protein SA homolog;
DE   Flags: Precursor;
GN   Name=ACSM3; Synonyms=SAH;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC       acyl-CoA, the first step in fatty acid metabolism (By similarity).
CC       Capable of activating medium-chain fatty acids with a preference for
CC       isobutyrate among fatty acids with 2-6 carbon atoms (By similarity).
CC       {ECO:0000250|UniProtKB:Q3UNX5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:46176, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57338, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46177;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57336, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181;
CC         Evidence={ECO:0000250|UniProtKB:Q3UNX5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q53FZ2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC         Evidence={ECO:0000250|UniProtKB:Q53FZ2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q53FZ2}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q3UNX5}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CR857411; CAH89702.1; -; mRNA.
DR   RefSeq; NP_001124772.1; NM_001131300.1.
DR   AlphaFoldDB; Q5REV5; -.
DR   SMR; Q5REV5; -.
DR   STRING; 9601.ENSPPYP00000008096; -.
DR   Ensembl; ENSPPYT00000008431; ENSPPYP00000008096; ENSPPYG00000007161.
DR   GeneID; 100171624; -.
DR   KEGG; pon:100171624; -.
DR   CTD; 6296; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000157930; -.
DR   HOGENOM; CLU_000022_59_10_1; -.
DR   InParanoid; Q5REV5; -.
DR   OMA; HAWSNLF; -.
DR   OrthoDB; 683933at2759; -.
DR   TreeFam; TF354287; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043759; F:methylbutanoate-CoA ligase activity; IEA:RHEA.
DR   GO; GO:0018729; F:propionate CoA-transferase activity; IEA:Ensembl.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:Ensembl.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..586
FT                   /note="Acyl-coenzyme A synthetase ACSM3, mitochondrial"
FT                   /id="PRO_0000306099"
FT   BINDING         235..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT   MOD_RES         106
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
FT   MOD_RES         157
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UNX5"
SQ   SEQUENCE   586 AA;  66060 MW;  A923438898F18582 CRC64;
     MLACVTMKML RHAKCFQRLA IFGSVRALHK DNRTATPQNF SNYESMKQDF KLGIPEYFNF
     AKDVLDQWTD KEKAGKKPSN PAFWWINRNG EEVRWSFEEL GSLSRKFANI LSEACSLQRG
     DRVILILPRV PEWWLANVAC LRTGTVLIPG TTQLTQKDIL YRLQSSKANC IITNDVLAPA
     VDAVAPKCEN LHSKLIVSEN SREGWGNLKE MMKHASDSHT CVKTKHNEIM AIFFTSGTSG
     YPKMTAHTHS SFGLGLSVNG RFWLDLTPSD VMWNTSDTGW AKSAWSSVFS PWIQGACVFT
     HHLPRFEPTS ILQTLSKYPI TVFCSAPTVY RMLVQNDMAS YKFKSLKHCV SAGEPITPDV
     TEKWRNKTGL DIYEGYGQTE TVLICGNFKG MKIKPGSMGK PSPAFDVKIV DVNGNVLPPG
     QEGDIGIQVL PNRPFGLFTH YVDNPSKTAS TLRGNFYITG DRGYMDEDGY FWFVARADDV
     ILSSGYRIGP FEVENALNEH PSVAESAVVS SPDPIRGEVV KAFVVLNPDY KSHDQEQLIK
     EIQEHVKKTT APYKYPRKVE FIQELPKTIS GKTKRNELRK KEWKTI
 
 
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