ID D5UWX9_TSUPD Unreviewed; 1105 AA.
AC D5UWX9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=Tpau_1373 {ECO:0000313|EMBL:ADG78001.1};
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS (Corynebacterium paurometabolum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG78001.1, ECO:0000313|Proteomes:UP000001213};
RN [1] {ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG78001.1, ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RX PubMed=21886861;
RA Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R.,
RA Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Tsukamurella paurometabola type strain (no.
RT 33).";
RL Stand. Genomic Sci. 4:342-351(2011).
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; CP001966; ADG78001.1; -; Genomic_DNA.
DR RefSeq; WP_013126039.1; NC_014158.1.
DR AlphaFoldDB; D5UWX9; -.
DR SMR; D5UWX9; -.
DR STRING; 521096.Tpau_1373; -.
DR KEGG; tpr:Tpau_1373; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG1022; Bacteria.
DR eggNOG; COG3320; Bacteria.
DR HOGENOM; CLU_009549_0_0_11; -.
DR Proteomes; UP000001213; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001213}.
FT DOMAIN 581..656
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 329
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 355
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 425
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 437..440
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 446
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 545
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 714..717
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 741
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 751
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 781..782
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 847
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 884
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 888
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 911
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT MOD_RES 615
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
SQ SEQUENCE 1105 AA; 118440 MW; 341F0A09BB618E2F CRC64;
MSIETVQNGV PAEGSVPPAD QQTERLPQVI ARIFAQFADR PAFATREAGP GTPYATVSYR
EIWRRVTALV ASWQSEVAPG DFVAILGFTS SDFVTVDLAT TLLGAPNVPL QAGAPAARIA
TILDETRPKI LAVSADQVDL AQEALAESAA TPRVVVFDGE RDGYEGIEAD ILSGSALPAP
EFFAPEPGTD PLVTLIYTSG STGTPKGAMY TEQLVRDAWL KVDSIVDIDM PAESLLHFLP
MSHMYGRNWL IAGLASGGTG YFAGASDMST LFDDLAAARP TAIGLVPRVC ELIHQRYLAV
EADTDAETAR VELRDRVLGG RLQAAMCGSA ALSSELQTFM EWLLGIDIQI GYGSTEAGGV
IRDGVVVRPP VTEYKLIDVP ELGYFVTDSP HPRGELLVKS TQLIPGYYNS DKRIRDDEGF
YRTGDVMAEL GPDRLEYVDR RSNVIKLAQG EFVPIAQLEA IYAAGPDVHQ IFLYGTSERS
YLIGVVVPAP GPDGETDAQT RTRVLDGLAA IARENDLAAY EVPRDVLIER DPFSQENGLR
SGIGKLVRPA LIARYGDRLH DLYAQADTRQ REGLRALDAS GPIIDTVLGA AALTLGADIA
DFDADTRFGD LGGDSLSALS LATTLEGLYD VPVPVQTIVG PTATLGGVAR HIEKARSGGV
AAPTADSVHG VGASVARATD LTLEKFIDPE LLALAPTLPA ATGEPNTVLL TGSTGYLGRF
LLLDWLRRVA PHGGTVIALV RGADADDARR RVTAAIGDSD PDLTQEFTSL AEHHLHVIAG
DFGSPALGLD DATWSDLAGR VDHVVHCGAL VNHVLPYDQL FGPNVVATGE VVRLALTTRR
KSVDYVSTVA VVPQDDGRVL VEDDDVRELG AERRIGADAY ANGYAVSKWA GEVLLHEAAD
LADLPVRVFR SDMILAHSRF HGQFNEVDQF TRLLLSIAET GLAPASFYTP DPSGHRPHYD
GLPVDFTAEA ITTLSAAGRS GYRTFHVLNA NDDGVSLDSF VDWIAASGRS IERIDDYDTW
FARFEQALQQ LPDEARQRSV LPLLHAVREP APAAGTSALS VDRFRGAVRE TGVGPGDIPV
LDRALIEKYL RDFETAGWLA PGARD
//
