ID Q9HTY7_PSEAE Unreviewed; 129 AA.
AC Q9HTY7;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Medium/long-chain acyl-CoA thioesterase YigI {ECO:0000256|ARBA:ARBA00040062};
DE EC=3.1.2.20 {ECO:0000256|ARBA:ARBA00038894};
GN OrderedLocusNames=PA5202 {ECO:0000313|EMBL:AAG08587.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG08587.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG08587.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007829|PDB:1ZKI}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RX PubMed=22439787; DOI=10.1042/BJ20112032;
RA Gonzalez C.F., Tchigvintsev A., Brown G., Flick R., Evdokimova E., Xu X.,
RA Osipiuk J., Cuff M.E., Lynch S., Joachimiak A., Savchenko A., Yakunin A.F.;
RT "Structure and activity of the Pseudomonas aeruginosa hotdog-fold
RT thioesterases PA5202 and PA2801.";
RL Biochem. J. 444:445-455(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20;
CC Evidence={ECO:0000256|ARBA:ARBA00035880};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + H2O = a long-chain fatty acid +
CC CoA + H(+); Xref=Rhea:RHEA:67680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139; Evidence={ECO:0000256|ARBA:ARBA00036002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain fatty acyl-CoA + H2O = a medium chain fatty
CC acid + CoA + H(+); Xref=Rhea:RHEA:68184, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558,
CC ChEBI:CHEBI:90546; Evidence={ECO:0000256|ARBA:ARBA00035781};
CC -!- SIMILARITY: Belongs to the YigI thioesterase family.
CC {ECO:0000256|ARBA:ARBA00038381}.
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DR EMBL; AE004091; AAG08587.1; -; Genomic_DNA.
DR PIR; E82995; E82995.
DR RefSeq; NP_253889.1; NC_002516.2.
DR RefSeq; WP_003096263.1; NZ_QZGE01000002.1.
DR PDB; 1ZKI; X-ray; 1.70 A; A/B=1-129.
DR PDBsum; 1ZKI; -.
DR AlphaFoldDB; Q9HTY7; -.
DR SMR; Q9HTY7; -.
DR STRING; 208964.PA5202; -.
DR PaxDb; 208964-PA5202; -.
DR DNASU; 878508; -.
DR GeneID; 878508; -.
DR KEGG; pae:PA5202; -.
DR PATRIC; fig|208964.12.peg.5452; -.
DR PseudoCAP; PA5202; -.
DR HOGENOM; CLU_089876_3_3_6; -.
DR InParanoid; Q9HTY7; -.
DR OrthoDB; 4565299at2; -.
DR PhylomeDB; Q9HTY7; -.
DR BioCyc; PAER208964:G1FZ6-5321-MONOMER; -.
DR EvolutionaryTrace; Q9HTY7; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016289; F:CoA hydrolase activity; IEA:UniProt.
DR CDD; cd03443; PaaI_thioesterase; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR NCBIfam; TIGR00369; unchar_dom_1; 1.
DR PANTHER; PTHR43240; 1,4-DIHYDROXY-2-NAPHTHOYL-COA THIOESTERASE 1; 1.
DR PANTHER; PTHR43240:SF20; MEDIUM_LONG-CHAIN ACYL-COA THIOESTERASE YIGI; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1ZKI};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438}.
FT DOMAIN 44..119
FT /note="Thioesterase"
FT /evidence="ECO:0000259|Pfam:PF03061"
SQ SEQUENCE 129 AA; 13814 MW; 52469532BB827C44 CRC64;
MSEMPAREQM ISAYSELVGL DPVSLGDGVA EVRLPMAAHL RNRGGVMHGG ALFSLMDVTM
GLACSSSHGF DRQSVTLECK INYIRAVADG EVRCVARVLH AGRRSLVVEA EVRQGDKLVA
KGQGTFAQL
//
