ID A9B3G8_HERA2 Unreviewed; 146 AA.
AC A9B3G8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Acyl-coenzyme A thioesterase THEM4 {ECO:0000256|ARBA:ARBA00040123};
DE EC=3.1.2.2 {ECO:0000256|ARBA:ARBA00038848};
DE AltName: Full=Thioesterase superfamily member 4 {ECO:0000256|ARBA:ARBA00043210};
GN OrderedLocusNames=Haur_1487 {ECO:0000313|EMBL:ABX04131.1};
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC Herpetosiphonaceae; Herpetosiphon.
OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX04131.1, ECO:0000313|Proteomes:UP000000787};
RN [1] {ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABX04131.1, ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RX PubMed=22675585; DOI=10.4056/sigs.2194987;
RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT "Complete genome sequence of the filamentous gliding predatory bacterium
RT Herpetosiphon aurantiacus type strain (114-95(T)).";
RL Stand. Genomic Sci. 5:356-370(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
CC Evidence={ECO:0000256|ARBA:ARBA00035852};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC Evidence={ECO:0000256|ARBA:ARBA00035852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000256|ARBA:ARBA00037002};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000256|ARBA:ARBA00037002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000256|ARBA:ARBA00036176};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate;
CC Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000256|ARBA:ARBA00035910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144;
CC Evidence={ECO:0000256|ARBA:ARBA00035910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000256|ARBA:ARBA00036930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000256|ARBA:ARBA00036930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000256|ARBA:ARBA00035835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000256|ARBA:ARBA00035835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000256|ARBA:ARBA00035827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000256|ARBA:ARBA00035827};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
CC -!- SIMILARITY: Belongs to the THEM4/THEM5 thioesterase family.
CC {ECO:0000256|ARBA:ARBA00038456}.
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DR EMBL; CP000875; ABX04131.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B3G8; -.
DR STRING; 316274.Haur_1487; -.
DR KEGG; hau:Haur_1487; -.
DR eggNOG; COG2050; Bacteria.
DR HOGENOM; CLU_089876_6_2_0; -.
DR InParanoid; A9B3G8; -.
DR BioCyc; HAUR316274:GHYA-1509-MONOMER; -.
DR Proteomes; UP000000787; Chromosome.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03443; PaaI_thioesterase; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR PANTHER; PTHR12418; ACYL-COENZYME A THIOESTERASE THEM4; 1.
DR PANTHER; PTHR12418:SF19; ACYL-COENZYME A THIOESTERASE THEM4; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 47..110
FT /note="Thioesterase"
FT /evidence="ECO:0000259|Pfam:PF03061"
SQ SEQUENCE 146 AA; 16244 MW; 0F35EE36BABFDD08 CRC64;
MNRQLDSQAC FVCGKNNPSG LQLDFFEEEK TVITRFVSTA LHQGWPGFVH GGIIATILDE
TLGRVGFLID AWTMTGRFEV RYRQPAPIDQ EITFTASMVR DRGRALEVEG FAQLPDGTIV
AEATGLYMRV SPELRATLSE QIAEGY
//
