ID A1KUS8_NEIMF Unreviewed; 160 AA. AC A1KUS8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 86. DE SubName: Full=Acyl-CoA hydrolase {ECO:0000313|EMBL:CAM10627.1}; GN OrderedLocusNames=NMC1417 {ECO:0000313|EMBL:CAM10627.1}; OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM OS 15464 / FAM18). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=272831 {ECO:0000313|EMBL:CAM10627.1, ECO:0000313|Proteomes:UP000002286}; RN [1] {ECO:0000313|EMBL:CAM10627.1, ECO:0000313|Proteomes:UP000002286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700532 / DSM 15464 / FAM18 RC {ECO:0000313|Proteomes:UP000002286}; RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023; RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., RA Quail M.A., Achtman M., Barrell B., Saunders N.J., Parkhill J.; RT "Meningococcal genetic variation mechanisms viewed through comparative RT analysis of serogroup C strain FAM18."; RL PLoS Genet. 3:230-240(2007). RN [2] {ECO:0007829|PDB:4IEN} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COENZYME A, AND RP DISULFIDE BONDS. RX PubMed=24192375; DOI=10.1107/S1744309113028042; RA Khandokar Y.B., Londhe A., Patil S., Forwood J.K.; RT "Expression, purification and crystallization of acetyl-CoA hydrolase from RT Neisseria meningitidis."; RL Acta Crystallogr. F Struct. Biol. Commun. 69:1303-1306(2013). CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family. CC {ECO:0000256|ARBA:ARBA00010458}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM421808; CAM10627.1; -; Genomic_DNA. DR RefSeq; WP_002216871.1; NC_008767.1. DR PDB; 4IEN; X-ray; 2.00 A; A/B/C/D=1-160. DR PDBsum; 4IEN; -. DR AlphaFoldDB; A1KUS8; -. DR SMR; A1KUS8; -. DR GeneID; 61281659; -. DR KEGG; nmc:NMC1417; -. DR HOGENOM; CLU_050164_3_0_4; -. DR BRENDA; 3.1.2.1; 3593. DR Proteomes; UP000002286; Chromosome. DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:InterPro. DR CDD; cd03442; BFIT_BACH; 1. DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1. DR InterPro; IPR040170; Cytosol_ACT. DR InterPro; IPR033120; HOTDOG_ACOT. DR InterPro; IPR029069; HotDog_dom_sf. DR InterPro; IPR006683; Thioestr_dom. DR PANTHER; PTHR11049; ACYL COENZYME A THIOESTER HYDROLASE; 1. DR PANTHER; PTHR11049:SF34; CYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE; 1. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1. DR PROSITE; PS51770; HOTDOG_ACOT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4IEN}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01106, KW ECO:0000313|EMBL:CAM10627.1}. FT DOMAIN 8..120 FT /note="HotDog ACOT-type" FT /evidence="ECO:0000259|PROSITE:PS51770" FT BINDING 5 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 29 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 56 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 64 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 65 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 78 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 81 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 85 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 86 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 87 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 93 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 109 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 111 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 138 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 141 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 146 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 149 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 157 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT BINDING 158 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0007829|PDB:4IEN" FT DISULFID 137 FT /note="Interchain (with C-158)" FT /evidence="ECO:0007829|PDB:4IEN" FT DISULFID 158 FT /note="Interchain (with C-137)" FT /evidence="ECO:0007829|PDB:4IEN" SQ SEQUENCE 160 AA; 17982 MW; 9EA969FF4903C27E CRC64; MTQQRQLPSH ELIMSELMMP DTANFSGNVH GGELLLLLDQ VAYSCASRYS GNYCVTLSVD KVLFKEPIHI GDLVTFYAAV NYTGRTSMEI GIRVEAQNIR TGEIRHTNSC YFTMVAVKDG KPVPVPPLEI LTDRQRCRYE KAKKRRDISL QASEDMSCGC //