ID A0A1A2UBP1_MYCSC Unreviewed; 1170 AA.
AC A0A1A2UBP1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A5679_02880 {ECO:0000313|EMBL:OBH85951.1};
OS Mycobacterium scrofulaceum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1783 {ECO:0000313|EMBL:OBH85951.1, ECO:0000313|Proteomes:UP000092207};
RN [1] {ECO:0000313|EMBL:OBH85951.1, ECO:0000313|Proteomes:UP000092207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2838 {ECO:0000313|EMBL:OBH85951.1,
RC ECO:0000313|Proteomes:UP000092207};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBH85951.1}.
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DR EMBL; LZJY01000431; OBH85951.1; -; Genomic_DNA.
DR RefSeq; WP_067310966.1; NZ_LZJY01000431.1.
DR AlphaFoldDB; A0A1A2UBP1; -.
DR Proteomes; UP000092207; Unassembled WGS sequence.
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 648..723
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT BINDING 294
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 389
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 410..411
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 415
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 488
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 500..503
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 509
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 609
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 780..783
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 807
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 817
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 847..848
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 873..875
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 913
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 949
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 953
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT MOD_RES 682
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
SQ SEQUENCE 1170 AA; 128675 MW; E5EA069CFE30C96B CRC64;
MSTINHDERL ERRIEDLTAN DPQFAAARPD PAVEAALERP GLRLPQVIRT VLDAYADRPA
LAHRAVEFVQ DSASGRTRLE LLSRFETLTY RELGERVSAL GRAWSNDEVH VGDRVCVLGF
NSVDYTTIDM ALATISAVSV PLQTSASLTS LHPIVAETEP TVIAASANQL PDAVELILGG
HRPTKLVVFD YHPEVDDERE AVETARARLA DTDVVVETLA EVLERGKALP DGPLPASEES
DPLALLIYTS GSTGAPKGAM YPQSNVAKIW RRGSRNWFGE SAASITLNFM PMSHVMGRGI
LYGTLGNGGT AYFAAKSDLS TLLEDLELVR PTELNFVPRI WETLFGEFQR LVERRLSEGG
DRAAVEAEVL ADQRQYLLGG RYIFAMTGSA PTSPELRTWV ESLLEMHLMD GYGSTEAGMV
LFDGEIQRPP VVDYKLVDVP DLGYFSTDRP HPRGELLLRT ENMFPGYYKR AETTANVFDE
DGYYRTGDVF AEVAPDKLVY VDRRNNVLKL AQGEFVTLAK LEAEFGNSPL VRQIYVYGNS
SQPYLLAVVV PTEEALASGD LETLKPQIAD SLQNVARQAG LQSYEVPRDF IIETTPFSLE
NGLLTGIRKL AWPKLKQHYG ERLERLYAEL AEGQANELAE LRRNGANAPV LQTVSRAAAA
MLGTASSELT PDAHFTDLGG DSLSALTFGN LLREIFDIDV PVGVIVSPAS DLQAIANYIE
GERQGTKRPT FAAVHGRDAT EVHASDLTLD KFLEAETLAA APSLPKPTTE VRTVLLTGAT
GFLGRYLALE WLERMDMVDG KVIALVRAKS DAEARGRLDK TFDSGDPKLL AHYRELAADH
LEVIAGDKGE ANLGLDSHTW QRLADTVDLI VDPAALVNHV LPYSELFGPN ALGTAELIRI
ALTTKLKPYT YVSTIGVGDQ IKPGQFVEDA DIRQISATRA INDNYANGYG NSKWAGEVLL
REAHDLCGLP VAVFRCDMIL ADTTYAGQLN LPDMFTRLML SLVATGVAPG SFYELDAEGN
RQRSHYDGLP VEFIAAAIST LGTQVLDNGK GFQTYHVMNP YDDGIGLDEY VDWLIEAGYG
IQRIADYGEW LRRFEQTMRG LPERQRQYSL LPLLHNYQKP EKPINGSMAP TDRFRAAVQE
AKIGPDKDIP HVSPPIIVKY ITDLQLLSLL
//
