MIG_MYCAV
ID MIG_MYCAV Reviewed; 550 AA.
AC O33855;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Medium-chain acyl-CoA ligase Mig {ECO:0000305};
DE EC=6.2.1.2 {ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
DE AltName: Full=Macrophage-induced gene {ECO:0000303|PubMed:7507894};
DE AltName: Full=Medium-chain fatty acid acyl-CoA synthetase {ECO:0000303|PubMed:11690636};
DE Flags: Precursor;
GN Name=mig {ECO:0000303|PubMed:7507894};
GN ORFNames=CKJ66_15745 {ECO:0000312|EMBL:PBA25886.1};
OS Mycobacterium avium.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1764;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=#5-8;
RX PubMed=9353032; DOI=10.1128/iai.65.11.4548-4557.1997;
RA Plum G., Brenden M., Clark-Curtiss J.E., Pulverer G.;
RT "Cloning, sequencing, and expression of the mig gene of Mycobacterium
RT avium, which codes for a secreted macrophage-induced protein.";
RL Infect. Immun. 65:4548-4557(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FLAC0165;
RA Caverly L.J., Spilker T., Lipuma J.;
RT "Phylogenetic analysis of Mycobacterium avium complex whole genomes.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RC STRAIN=#5-8;
RX PubMed=7507894; DOI=10.1128/iai.62.2.476-483.1994;
RA Plum G., Clark-Curtiss J.E.;
RT "Induction of Mycobacterium avium gene expression following phagocytosis by
RT human macrophages.";
RL Infect. Immun. 62:476-483(1994).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=#5-8;
RX PubMed=11690636; DOI=10.1016/s0167-4781(01)00287-1;
RA Morsczeck C., Berger S., Plum G.;
RT "The macrophage-induced gene (mig) of Mycobacterium avium encodes a medium-
RT chain acyl-coenzyme A synthetase.";
RL Biochim. Biophys. Acta 1521:59-65(2001).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19477415; DOI=10.1016/j.chembiol.2009.03.012;
RA Leger M., Gavalda S., Guillet V., van der Rest B., Slama N., Montrozier H.,
RA Mourey L., Quemard A., Daffe M., Marrakchi H.;
RT "The dual function of the Mycobacterium tuberculosis FadD32 required for
RT mycolic acid biosynthesis.";
RL Chem. Biol. 16:510-519(2009).
CC -!- FUNCTION: Catalyzes the activation of medium-chain fatty acids as acyl-
CC coenzyme A (acyl-CoA) (PubMed:11690636, PubMed:19477415). Shows maximal
CC activity with saturated fatty acids of medium-chain length between C6
CC and C12. Has lower activity with tridecanoic acid (C13), tetradecanoic
CC acid (C14) and with unsaturated fatty acids like oleic acid (C18:1),
CC linolenic acid (C18:3) and arachidonic acid (C20:4). Shows weak
CC activity with some aromatic carbon acids (PubMed:11690636). Involved in
CC the metabolism of fatty acid during mycobacterial survival in
CC macrophages (PubMed:11690636). {ECO:0000269|PubMed:11690636,
CC ECO:0000269|PubMed:19477415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA;
CC Xref=Rhea:RHEA:44088, ChEBI:CHEBI:30616, ChEBI:CHEBI:32362,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44089;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636,
CC ECO:0000269|PubMed:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636,
CC ECO:0000269|PubMed:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:11690636};
CC -!- ACTIVITY REGULATION: Inhibited by 2-hydroxydodecanoic acid, a typical
CC inhibitor of medium-chain acyl-CoA synthetases.
CC {ECO:0000269|PubMed:11690636}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=285 uM for octanoic acid {ECO:0000269|PubMed:11690636};
CC KM=1775 uM for decanoic acid {ECO:0000269|PubMed:11690636};
CC KM=20 uM for dodecanoic acid {ECO:0000269|PubMed:11690636};
CC KM=36 uM for ATP {ECO:0000269|PubMed:11690636};
CC KM=45 uM for CoA {ECO:0000269|PubMed:11690636};
CC Vmax=183 nmol/min/mg enzyme with octanoic acid as substrate
CC {ECO:0000269|PubMed:11690636};
CC Vmax=510 nmol/min/mg enzyme with decanoic acid as substrate
CC {ECO:0000269|PubMed:11690636};
CC Vmax=163 nmol/min/mg enzyme with dodecanoic acid as substrate
CC {ECO:0000269|PubMed:11690636};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:11690636}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9353032}.
CC -!- INDUCTION: Expression is induced in human macrophages (PubMed:7507894,
CC PubMed:9353032). Induced by acidity (PubMed:9353032). Transcription
CC seems to be maximal between day 1 and day 5 after phagocytosis
CC (PubMed:7507894). {ECO:0000269|PubMed:7507894,
CC ECO:0000269|PubMed:9353032}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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; U43598; AAB87139.2; -; Genomic_DNA.
DR EMBL; NSFD01000040; PBA25886.1; -; Genomic_DNA.
DR RefSeq; WP_033717924.1; NZ_NSFM01000003.1.
DR AlphaFoldDB; O33855; -.
DR SMR; O33855; -.
DR SwissLipids; SLP:000000974; -.
DR EnsemblBacteria; PBA25886; PBA25886; CKJ66_15745.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000217768; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell wall; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..550
FT /note="Medium-chain acyl-CoA ligase Mig"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451972"
SQ SEQUENCE 550 AA; 58582 MW; C08E3A472C8A247B CRC64;
MSDTTTAFTV PAVAKAVAAA IPDRELIIQG DRRYTYRQVI ERSNRLAAYL HSQGLGCHTE
REALAGHEVG QDLLGLYAYN GNEFVEALLG AFAARVAPFN VNFRYVKSEL HYLLADSEAT
ALIYHAAFAP RVAEILPELP RLRVLIQIAD ESGNELLDGA VDYEDALASV SAQPPPVRHC
PDDLYVLYTG GTTGMPKGVL WRQHDIFMTS FGGRNLMTGE PSSSIDEIVQ RAASGPGTKL
MILPPLIHGA AQWSVMTAIT TGQTVVFPTV VDHLDAEDVV RTIEREKVMV VTVVGDAMAR
PLVAAIEKGI ADVSSLAVVA NGGALLTPFV KQRLIEVLPN AVVVDGVGSS ETGAQMHHMS
TPGAVATGTF NAGPDTFVAA EDLSAILPPG HEGMGWLAQR GYVPLGYKGD AAKTAKTFPV
IDGVRYAVPG DRARHHADGH IELLGRDSVC INSGGEKIFV EEVETAIASH PAVADVVVAG
RPSERWGQEV VAVVALSDGA AVDAGELIAH ASNSLARYKL PKAIVFRPVI ERSPSGKADY
RWAREQAVNG
