FAA10_MYCTO
ID FAA10_MYCTO Reviewed; 540 AA.
AC P9WQ54; F2GLP5; L0T2G2; Q10878; Q7DAH0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase FadD10 {ECO:0000250|UniProtKB:P9WQ55};
DE EC=6.2.1.20 {ECO:0000250|UniProtKB:P9WQ55};
DE EC=6.2.1.47 {ECO:0000250|UniProtKB:P9WQ55};
GN Name=fadD10; OrderedLocusNames=MT0108;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as
CC acyl-adenylates (acyl-AMP), which are then transferred to the
CC phosphopantetheine arm of the acyl carrier protein (ACP) MT0109.
CC {ECO:0000250|UniProtKB:P9WQ55}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.47;
CC Evidence={ECO:0000250|UniProtKB:P9WQ55};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50461;
CC Evidence={ECO:0000250|UniProtKB:P9WQ55};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC Evidence={ECO:0000250|UniProtKB:P9WQ55};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589;
CC Evidence={ECO:0000250|UniProtKB:P9WQ55};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:P9WQ55}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQ55}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WQ55}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK44330.1; -; Genomic_DNA.
DR PIR; C70751; C70751.
DR RefSeq; WP_003400792.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ54; -.
DR SMR; P9WQ54; -.
DR EnsemblBacteria; AAK44330; AAK44330; MT0108.
DR KEGG; mtc:MT0108; -.
DR PATRIC; fig|83331.31.peg.113; -.
DR HOGENOM; CLU_000022_59_0_11; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding.
FT CHAIN 1..540
FT /note="Medium/long-chain-fatty-acid--[acyl-carrier-protein]
FT ligase FadD10"
FT /id="PRO_0000426835"
FT BINDING 315..316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQ55"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQ55"
SQ SEQUENCE 540 AA; 56590 MW; 015A8EDD824964C8 CRC64;
MGGKKFQAMP QLPSTVLDRV FEQARQQPEA IALRRCDGTS ALRYRELVAE VGGLAADLRA
QSVSRGSRVL VISDNGPETY LSVLACAKLG AIAVMADGNL PIAAIERFCQ ITDPAAALVA
PGSKMASSAV PEALHSIPVI AVDIAAVTRE SEHSLDAASL AGNADQGSED PLAMIFTSGT
TGEPKAVLLA NRTFFAVPDI LQKEGLNWVT WVVGETTYSP LPATHIGGLW WILTCLMHGG
LCVTGGENTT SLLEILTTNA VATTCLVPTL LSKLVSELKS ANATVPSLRL VGYGGSRAIA
ADVRFIEATG VRTAQVYGLS ETGCTALCLP TDDGSIVKIE AGAVGRPYPG VDVYLAATDG
IGPTAPGAGP SASFGTLWIK SPANMLGYWN NPERTAEVLI DGWVNTGDLL ERREDGFFYI
KGRSSEMIIC GGVNIAPDEV DRIAEGVSGV REAACYEIPD EEFGALVGLA VVASAELDES
AARALKHTIA ARFRRESEPM ARPSTIVIVT DIPRTQSGKV MRASLAAAAT ADKARVVVRG
