ID A0A0E3XNJ2_MYCCH Unreviewed; 1187 AA.
AC A0A0E3XNJ2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Carboxylic acid reductase {ECO:0000256|HAMAP-Rule:MF_02247};
DE Short=CAR {ECO:0000256|HAMAP-Rule:MF_02247};
DE EC=1.2.1.- {ECO:0000256|HAMAP-Rule:MF_02247};
DE AltName: Full=ATP/NADPH-dependent carboxylic acid reductase {ECO:0000256|HAMAP-Rule:MF_02247};
GN Name=car {ECO:0000256|HAMAP-Rule:MF_02247};
GN ORFNames=GR01_14065 {ECO:0000313|EMBL:AKC39458.1};
OS Mycobacteroides chelonae (Mycobacterium chelonae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=1774 {ECO:0000313|EMBL:AKC39458.1, ECO:0000313|Proteomes:UP000033056};
RN [1] {ECO:0000313|EMBL:AKC39458.1, ECO:0000313|Proteomes:UP000033056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35752 {ECO:0000313|EMBL:AKC39458.1,
RC ECO:0000313|Proteomes:UP000033056};
RX PubMed=26021923;
RA Hasan N.A., Davidson R.M., de Moura V.C., Garcia B.J., Reynolds P.R.,
RA Epperson L.E., Farias-Hesson E., DeGroote M.A., Jackson M., Strong M.;
RT "Draft Genome Sequence of Mycobacterium chelonae Type Strain ATCC 35752.";
RL Genome Announc. 3:e00536-15(2015).
CC -!- FUNCTION: Catalyzes the ATP- and NADPH-dependent reduction of
CC carboxylic acids to the corresponding aldehydes. {ECO:0000256|HAMAP-
CC Rule:MF_02247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde +
CC diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_02247};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02247};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000256|HAMAP-
CC Rule:MF_02247};
CC -!- DOMAIN: The N-terminal domain likely catalyzes substrate activation by
CC formation of an initial acyl-AMP intermediate, the central region
CC contains the phosphopantetheine attachment site, and the C-terminal
CC domain catalyzes the reduction by NADPH of the intermediate thioester
CC formed from the attack of the phosphopantetheine thiol at the carbonyl
CC carbon of acyl-AMP. {ECO:0000256|HAMAP-Rule:MF_02247}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Carboxylic acid reductase subfamily. {ECO:0000256|HAMAP-Rule:MF_02247}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02247}.
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DR EMBL; CP010946; AKC39458.1; -; Genomic_DNA.
DR RefSeq; WP_046254020.1; NZ_MLCH01000017.1.
DR AlphaFoldDB; A0A0E3XNJ2; -.
DR GeneID; 31680460; -.
DR PATRIC; fig|1774.35.peg.2855; -.
DR HOGENOM; CLU_009549_0_0_11; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000033056; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd17632; AFD_CAR-like; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_02247; Carbox_acid_reduct; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR046407; CAR.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; NF041592; carboxyl_red; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR43272:SF52; CARBOXYLIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02247};
KW NADP {ECO:0000256|HAMAP-Rule:MF_02247};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02247};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02247};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|HAMAP-
KW Rule:MF_02247};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_02247}.
FT DOMAIN 659..734
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT BINDING 301
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 398
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 419..420
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 424
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 497
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 518
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 620
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 792..795
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 819
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 829
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 885..887
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 925
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 961
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 965
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 988
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT MOD_RES 693
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
SQ SEQUENCE 1187 AA; 128442 MW; AC3C6A55644424B6 CRC64;
MTVNNDTDLQ LEQLTRRIEN LRESDPQFRD TLPDPAVAQQ VLRPGLHLSE AIATLMTGYA
ARPALGERAR ELVTDHDGRT IQRLLPRFET TTYGELWSRT TSVAASWHHD TAHPVKGGDL
VATLGFTSID YTVLDLAIMI LGGVAVPLQT SAPASQWTTI LAEAEPNTLA VSVELIGVAL
ESVLATPSIK QVVVFDYTPE VDAQREAFDA AGARLAGTGV AIETLDAVIA RGADLPAAPL
YAPSPGDDPL ALLIYTSGST GAPKGAMHSE NIVRRWWIRE DVMAGTENLP MIGLNFMPMS
HIMGRGTLTS TLSTGGLGYF AASSDMSTLF EDMELIRPTA LALVPRVCDM VFQRFQTEVD
RRLAGAHTAD ANTVAAEVKA EIRDSLFGGR VLAVMVGSAP LSDELGEFIE SCFELHLTDG
YGSTEAGMVF RDGIVQRPPV IEYKLVDVPE LGYFSTDQPH PRGELLLKTD GMFLGYYKRP
EVTAGVFDEN GFYMTGDIVT ELAHDNIRIV DRRNNVLKLS QGEFVAVATL EAEYANSPVV
HQIYVYGSSE RSYLLAVVVP TPQAVAAAKG DETALKATIA ESLQDIAREL QLQSYEIPRD
FIIEPQPFTQ GNGLLTGIAK LARPNLKAHY GDRLEQMYAD IAEQQAAELR ALHSVDPDKP
ALETVLKAAQ ALLGVSSAEL AAYAHFTDLG GDSLSALSFS DLLRDIFGVE VPVGVIVSAA
NDLGGVAQFI DEQRHSGGTR PTADTVHGAG HTEIRAADLT LDKFIDEATL RAAPALPRST
GTPQTVLLTG SNGYLGHYLA LEWLERLDKT DGKLIVIVRG KDAQAAYHRL EEAFDTGDAG
LLTHFRALAD KHLEVLAGDI GDPNLGLDAD TWQRLADTVD VIVHPAALVN HVLPYRQLFG
PNVVGTAEII KLALTTKIKP VTYLSTVAVA AYVDPSTFDE ESDIRLISAV RPVDELYANG
YGNSKWAGEV LLREAHDLCG LPVAVFRSDM ILAHSHYTGQ LNVPDQFTRL ILSLIATGIA
PGSFYQAQAT GERPRAHYDG LPGDFTAEAI TTLGTQVPEG PEAYVTYDCV NPHSDGISLD
NFVDWLIDAG YPIQRIDNYG DWFDRFDTAI RGLPEKQKQH SLLPLLHAFE QPSGADDHGV
VPAKRFQHAV QAAGIGPVGQ DGTTDIPHLS QQLIVKYATD LEQLGLL
//
