ID A0A1E8Q6I1_9MYCO Unreviewed; 1167 AA.
AC A0A1E8Q6I1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BEL07_09285 {ECO:0000313|EMBL:OFJ54086.1};
OS Mycobacterium grossiae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1552759 {ECO:0000313|EMBL:OFJ54086.1, ECO:0000313|Proteomes:UP000178953};
RN [1] {ECO:0000313|EMBL:OFJ54086.1, ECO:0000313|Proteomes:UP000178953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCH {ECO:0000313|EMBL:OFJ54086.1,
RC ECO:0000313|Proteomes:UP000178953};
RA Greninger A.L., Qin X., Jerome K., Vora S., Quinn K.;
RT "genome sequence of Mycobacterium sp. 739 SCH.";
RL Submitted (SEP-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:OFJ54086.1}.
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DR EMBL; MCHX01000017; OFJ54086.1; -; Genomic_DNA.
DR RefSeq; WP_070352844.1; NZ_MCHX01000017.1.
DR AlphaFoldDB; A0A1E8Q6I1; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000178953; 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}; Reference proteome {ECO:0000313|Proteomes:UP000178953}.
FT DOMAIN 643..718
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT BINDING 292
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 384
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 405..406
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 410
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 483
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 495..498
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 504
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 604
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 776..779
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 803
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 813
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 843..844
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 869..871
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 909
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
FT BINDING 945
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 MOD_RES 677
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02247"
SQ SEQUENCE 1167 AA; 126237 MW; 0348675BC079E540 CRC64;
MSTDTREARY ERRIADLHAN DPQFAAAAPD ESVGAAVVGK PLPEVVRTVL EAYADRPALG
QRAADYRIDD TGRTVAALQN RFETITYGEL AARVNAVAVA LADQPVRPGD RVAILGFTSI
DYTVVDTATT QLAAVSVPLQ TSAAIAQLQP IIAETEPSVI ASSIDYLDDA VALVEAGPAP
ARLVVFDVRP EVDDHRDALA AATARLADAD VVVETLADVL ARGRDAAVPT GRTADDDLAL
LIYTSGSTGA PKGAIYPRHK VAEMWTAANL NHWDETQGAV PSITLNFLPM SHVMGRGVLY
ATLAAGGTAY FAARSDLSTF LEDLALVRPT QMNFVPRIWD MLHQEYESEV ARRQATSDED
RQRVLADLRQ NLLGGRYVSA ITGSAPIAPE LKAWVEDLLD MHLIEGYGST EAGAVFVDGQ
VRRPPVLEYK LIDVPDLGYF TTDVPHPRGE LLVKSEQLFP GYYKRPEVTA EVFDADGFYR
TGDVVAETGP DQLRYVDRRN NVLKLSQGEF VTVSKLEAVF TGSALVRQIF LYGNSARPYL
LAVVVPTEEA QARYSGDDLK KAVSASLKDA ARSADLQSYE IPRDVIIETE PFTVENGLLT
GIRKLAWPRL KERYGAALEQ LYLDLSEGQA DELRALRRNG AEGPVLDTVS RAAKALLGAA
ASDVSADAHF TDLGGDSLSA LTFANLLHEI FSVDVPVGVI VSPASDLAAI AAYVEAEQSG
ASKRPTYAAV HGRDATEVLA SDLTLEKFID AETLAAARQL PAPGGDIRTV LLTGATGFLG
RYLALEWLER MALVDGTVVC LVRGRSDEDA RRRLDATFDS GDETLLAHYR ELAAKHLEVI
AADKGEPNLG LDQATWQRLA DTVDFIVDPA ALVNHVLPYS QLFGPNALGT AELIRLAITS
KIKPFAYVST IGVAWGVAPG QFTEDADVRE MSPSRAISDA YANGYGTSKW AGEVLLREAN
DLCGLPVSVF RCDMILADTT YAGQLNLPDM FTRMMLSLVA TGVAPESFYE LDAEGNRQRA
HYDGLPVEFI AEAISTLGVD VAAAGSGAFE TYHVMNPHDD GIGMDQFVDW LIEAGFPISR
VGDYAAWLDR FSTTLRGLPE RQRNASLLPL LHNYQKPEHP MAGSVAPVER FRPAVQDAKI
GPDKDIPHVT KPVIVKYVTD LQLLGLL
//
