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Database: UniProt
Entry: V6K233_STRNV
LinkDB: V6K233_STRNV
Original site: V6K233_STRNV 
ID   V6K233_STRNV            Unreviewed;       152 AA.
AC   V6K233;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=M877_28230 {ECO:0000313|EMBL:EST23009.1};
OS   Streptomyces niveus NCIMB 11891.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST23009.1, ECO:0000313|Proteomes:UP000017971};
RN   [1] {ECO:0000313|EMBL:EST23009.1, ECO:0000313|Proteomes:UP000017971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST23009.1,
RC   ECO:0000313|Proteomes:UP000017971};
RX   PubMed=24407644;
RA   Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT   Aminocoumarin Antibiotic Novobiocin.";
RL   Genome Announc. 2:e01146-e01113(2014).
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}.
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:EST23009.1}.
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DR   EMBL; AWQW01000202; EST23009.1; -; Genomic_DNA.
DR   RefSeq; WP_023541741.1; NZ_CM002280.1.
DR   AlphaFoldDB; V6K233; -.
DR   STRING; 193462.BBN63_28825; -.
DR   PATRIC; fig|1352941.4.peg.5739; -.
DR   eggNOG; COG2050; Bacteria.
DR   HOGENOM; CLU_089876_5_1_11; -.
DR   OrthoDB; 9806185at2; -.
DR   Proteomes; UP000017971; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          57..126
FT                   /note="Thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF03061"
SQ   SEQUENCE   152 AA;  16335 MW;  37C9DAAC3E88BA2D CRC64;
     MEDRMQHEQA SPAVQKRVQD SFDLQGLMSH LGARLTHIGP GRVHITLPAR PEVTQQHGYI
     HAGATSAIAD SAGGYAALTL FDEDCDVLTV EYKINLLAPA AGDHLEAIGT VLKPGRTLTV
     CQLEVYGVQA DGARKLVANG QQTLIRVNRT AQ
//
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