ID A0A0F2RRC8_9PROT Unreviewed; 1788 AA.
AC A0A0F2RRC8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=VR70_05575 {ECO:0000313|EMBL:KJS40586.1};
OS Rhodospirillaceae bacterium BRH_c57.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae.
OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS40586.1, ECO:0000313|Proteomes:UP000033468};
RN [1] {ECO:0000313|EMBL:KJS40586.1, ECO:0000313|Proteomes:UP000033468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS40586.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
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:KJS40586.1}.
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DR EMBL; LAEA01000087; KJS40586.1; -; Genomic_DNA.
DR STRING; 1629718.VR70_05575; -.
DR PATRIC; fig|1629718.3.peg.2684; -.
DR Proteomes; UP000033468; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1205..1554
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 1788 AA; 192492 MW; 3E18DC312B088E20 CRC64;
MADAVFTPPL PGTVRINPVR DGKTWQAMRE ACAADPGAFH GAVAARNIHW FHPGSNAWLT
QTDDGAWTGF DAATGAAVTL GGAWTPWDKA FDDSDAPIYR WFSGGLTNAA FNEVDRHVLA
GHGAEVAYWY EGDRWDADAN GGTGGPVHHR TLTRRDLFVQ SVIAAVALRT LGLGKGDCIA
FNMPNILDQI VWTEAAKRLG VIYTPVFGGF SDKTLSDRIE NAGARVVITA DGASRNAEVV
PFKEAYTDPA LDRFVAFPDA LRTLRAVAED KAGHGIAAEL LAAAEAALKG EITVAPADVM
RAVGRVLDKP GLLDAEAAAT LRADIAEALA ATKRRIDHVV VVRHAHLPDM PWTEGRDLWA
HDLLAEAAKV VGNVDGLDGA DLAAALWKAC PPEPVDAEFP LFIMYTSGST GKPKGVVHVH
GGYVSGLIET MKVSFDAVPG EDVMYVVADP GWITGQSYLI TAALAHRIPG IVTEGAPVFP
NAGRFSNILE RHGCTIFKAG ATFLKSIMTH PLDREDVAKA DMGRVKVATF CAEPTSPAVQ
QFAMDLITPQ YINSYWATEH GGIVWTHPYG NADQPLRADA HTWPLPWVMG DVWLPEGEHD
LNGRVGFRPA EDGEKGEIVV TAPYPYLART IWGHPEGVGS PAWKGDADRW TQTYYGRFRD
LGGVPQWAYL QGDFAVRYED GSYTLHGRSD DVINVSGHRM GTEEIEGAIL KDKAVNPDSP
VGNCIVIGAP HRDKGLTPVA FVLPAKGRTL TMDDERRLKD LVRAEKGAVA VPSDFIAVSA
FPETRSGKYM RRFLKALMLD EPLGDTSTLR NPEIMPEIET AITAWKRGQA RADAQRVIET
TRSLRVQYDT VAEGRVVATL TIGNPPVNAL SERVLDELDT TIAHLGRRAD VRAVVICGQG
NRTFVAGADI RQMQDEVNSV EEARALPAKA HRVFDAIERL GKPVVAAVQG VALGGGCELA
MACHLRIGDA RTRMGQPEVN LFLPPGYGGT QRLPRLLAAK DPERGVGDAL RILLSGRQVD
ARAAMRLGLL DYVCVGSEDP VSVAQAMARM AAAGKGGPAH DALTARLEAV AEWEKPGTVP
DVDVQPLLDQ AESVGRGVVA RAIVDLVRRG LSEGFSAGLK AERDAFARLL LDAEHGARKG
IALFLDKKSP PLPARPRPEF TPEEAERLGV LPVGSPFIPG VDALPEWQWA WGAVRDATTG
AARHGDPKDA EVRALIPVPE PTSNQALVYV LASEINYNDI WALTGIPISL FDEHDEDVHV
TGSGGVGMVV RLGEGLQAEG RLSVGQLVSV YSGVSDLLDP RAGADPMFTN FHIQGYQSPD
GSHQQFMLAD GPQLFPLVPD LDLEVAGSYM LTAGTAYRAL FTTLGVRPGK RLFVEGAASG
TGAFCLELGL AARLAVTGMV SSEDRAEAVE ALGAAAINRR DRELTNRFTR VPVDPVEVID
WEAKGGHWVE SIRKRNDGHL VDYAVSHAGE TAFPRTFQAL APGGVLTFYG ASSGYHMTFL
GKEGSAEAAD MLHRAALRPG EAVVVFYGTG THQRDNTALA AIEAARAGGG RIVAVTDTDA
ERDFILSLGF GDAVLGAVSL AEIKRRHPHF SWPDTMPDLP DPQAETAAFK ETVRRFTEDT
FKPLGQAVGK FLRSSANPRG TPDIVVERAH VDTLAWSTML VSPEAGRVVY IGDMAPRGRA
RRYSFYAPQV WMRQRRIYMP TAGIFGSHLS NAAEMIGLNR MIAGGTLRVP QPYLGAWDDL
PGLHQAMWEN RLREVTNGAA NAVVNHALPE PGLRSRDELI AAWAAGRG
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