ID A2SCL6_METPP Unreviewed; 571 AA. AC A2SCL6; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE SubName: Full=Putative acetyl-coenzyme A synthetase {ECO:0000313|EMBL:ABM93305.1}; DE EC=6.2.1.1 {ECO:0000313|EMBL:ABM93305.1}; GN OrderedLocusNames=Mpe_A0343 {ECO:0000313|EMBL:ABM93305.1}; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Sphaerotilaceae; Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM93305.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM93305.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1 RC {ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000256|ARBA:ARBA00006432}. 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; CP000555; ABM93305.1; -; Genomic_DNA. DR RefSeq; WP_011827944.1; NC_008825.1. DR AlphaFoldDB; A2SCL6; -. DR STRING; 420662.Mpe_A0343; -. DR KEGG; mpt:Mpe_A0343; -. DR eggNOG; COG0365; Bacteria. DR HOGENOM; CLU_000022_59_10_4; -. DR Proteomes; UP000000366; Chromosome. DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com. DR InterPro; IPR042099; ANL_N_sf. DR PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1. DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABM93305.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}. FT DOMAIN 53..393 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 457..535 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 571 AA; 62790 MW; BDA321EFCD59426F CRC64; MTSAVPFLQA RDLLLRLRDD QAAAAREFRW PALGEFNWAL DHFDAMARDP ARADAPALWI VGEDGSEVKR SFRELSQRSA QVANHLRALG VRRGDRVLLM LGNELALWET MLAAMKLGAV LIPATALLTT EDLRDRMERG DVRHVVTASA QTDKFAPLPG DYTRISIGEA QPGWQRFEDA AAAPSAFTPD GPTRASDPLL LYFTSGTTSK PKLVLHTHQS YPVGHLSTMY WIGLRPGDVH LNISSPGWAK HAWSCFFAPW NAGACVFIYN TARFNAGGLL AVLERCRVTS LCAPPTVWRM MVQEDLGAYR GRLALRELIG AGEPLNPEII EQVRAAWDMT VRDGYGQTET TAQIGNAPGQ PLKPGSMGRP LPGYRIALID ADGKEADEGE VCIVLAERPL GLMVGYQDSA EKTADAMRDG YYHTGDVAAR DAEGYITFVG RADDVFKASD YRISPFELES ALIEHEAVAE VAVVPSPDPL RLAVPKAYLI LTAGQTPDRA LAEAILGFAR KQLAPYKRVR RIEFVTELPK TISGKIRRVQ LRAQEVERRA AGVRAAGEFF EEDFPQLKAE A //