ID   F7ZGN1_ROSLO            Unreviewed;       565 AA.
AC   F7ZGN1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   02-SEP-2026, entry version 53.
DE   RecName: Full=3-methylmercaptopropionyl-CoA ligase {ECO:0000256|ARBA:ARBA00067668};
DE            EC=6.2.1.44 {ECO:0000256|ARBA:ARBA00066616};
GN   Name=fadK2 {ECO:0000313|EMBL:AEI92331.1};
GN   OrderedLocusNames=RLO149_c003010 {ECO:0000313|EMBL:AEI92331.1};
OS   Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS   15278 / OCh 149).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI92331.1, ECO:0000313|Proteomes:UP000001353};
RN   [1] {ECO:0000313|EMBL:AEI92331.1, ECO:0000313|Proteomes:UP000001353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC   {ECO:0000313|Proteomes:UP000001353};
RX   PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA   Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA   Daniel R., Simon M., Brinkhoff T.;
RT   "Comparative genome analysis and genome-guided physiological analysis of
RT   Roseobacter litoralis.";
RL   BMC Genomics 12:324-324(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(methylsulfanyl)propanoate + ATP + CoA = 3-
CC         (methylsulfanyl)propanoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:43052, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:49016, ChEBI:CHEBI:57287, ChEBI:CHEBI:82815,
CC         ChEBI:CHEBI:456215; EC=6.2.1.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00051915};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43053;
CC         Evidence={ECO:0000256|ARBA:ARBA00051915};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP002623; AEI92331.1; -; Genomic_DNA.
DR   RefSeq; WP_013960274.1; NC_015730.1.
DR   AlphaFoldDB; F7ZGN1; -.
DR   STRING; 391595.RLO149_c003010; -.
DR   KEGG; rli:RLO149_c003010; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_7_5; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000001353; Chromosome.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:TreeGrafter.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:TreeGrafter.
DR   CDD; cd05917; FACL_like_2; 1.
DR   FunFam; 3.30.300.30:FF:000008; 2,3-dihydroxybenzoate-AMP ligase; 1.
DR   FunFam; 3.40.50.12780:FF:000003; Long-chain-fatty-acid--CoA ligase FadD; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-b_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; NF009233; PRK12583.1; 1.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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:AEI92331.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001353}.
FT   DOMAIN          33..422
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          473..548
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   565 AA;  61679 MW;  2634BFBF0610C886 CRC64;
     MSALGRQPQN NLSHVYGSTA DALWNLTIPQ LLAQTAARLP DHPAAVFTRQ AIRWTYRDFV
     REVDRLAAGL LTLGIEKGDR VGIWAPNCAE WLLTQFATAR IGAILVCINP AYRLSELEYA
     LNKVGCSALV MAPRHKSSDY VAMLTELMPE LANATPGQCQ AARVPKLRHV IVTGDAPPEG
     TIGFDAICAA GSAVPVETLD RISNDLSPQD AINIQFTSGT TGSPKGACLT HHNIVNNAHF
     VTQTMQFTEE DRLCIPVPFY HCFGMVMGTL GCVSKGATMV IPGEGFDARA TLEAVTQEKC
     TALYGVPTMF VNALELADFD TFDLSSLRTG IMAGAPCPIE VMRQVQARMH MQGVTIAYGM
     TETSPVSFQS NMDDPLEKRV SSVGRIHPHV EVKIVDDTGN TVKTGEQGEL LTRGYSVMQG
     YWEDDAQTAA SIDAQGWMHT GDLARLDADG FCTITGRLKD MILRGGENIY PREIEEFLYT
     HPDILQAQVF GIPDNKLGEA VCAWIVARAG SDLAETDVQD FCRSAIAHFK VPAYVSFKDE
     LPMTVTGKPQ KFVMRDRMIK ELGRG
//