ID A0A0U5BH72_9BACL Unreviewed; 1804 AA.
AC A0A0U5BH72;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN Name=acs {ECO:0000313|EMBL:BAU29623.1};
GN ORFNames=CB4_03834 {ECO:0000313|EMBL:BAU29623.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU29623.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU29623.1, ECO:0000313|Proteomes:UP000217696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU29623.1,
RC ECO:0000313|Proteomes:UP000217696};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-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};
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DR EMBL; AP017312; BAU29623.1; -; Genomic_DNA.
DR KEGG; asoc:CB4_03834; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000217696; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 2.
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; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 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, ECO:0000313|EMBL:BAU29623.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000217696}.
FT DOMAIN 1221..1573
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 1804 AA; 201675 MW; 5691676A2A395616 CRC64;
MDVRTQKAKS NPILTREDWN KQRHLAEQDP GNFHGDIAKR EIHWYDEQAN AWMIWNDEHN
QWMGLDADTG APVTVTHSPA YEPWKTAFDD SDAPFYKWFS GGLTNACFNE VDRHVMNGHG
DEIAFYFEGD RWDQAKNDGR GGPVVEFAVT RKQLMLETLK AAQVFKNLGL KKGDRIALNM
PNIMEQIYYT EAAKRLGIVY TAVFGGFSDK TLSDRIHNAG AKVVITSDGG YRNAQIVEFK
EAYTDPALDN YVPKEIAVQI VEEKLKELNL NEQQSTLIQE KVMQTIGSEI TVERSDAMRG
VGMALAQFHD MDAEQKSHIR TVIAKGLVDA PPRVEAVIVV RHTRQQDLNW RPERDRWSHE
LIGEAVEQIL AIAREQGTNV ANEQDLLALP TEDFIRIMYA VSKPEPVDAE YPLFIIYTSG
STGKPKGVVH VHGGYTAGLA HTMKVSFDAT PGEDIMYVIA DPGWITGQSY LISASLTTRT
TSIVAEGAPV FPSAGRYASI IERYNVTIFK AGSTFLKTIM SNPQNKADVE QYSMDTLRVA
TFCAEPTSPA VQQFGMDLMT PQYINSYWAT EHGGIVWTHF FGNNDFQLKA DAHTFPLPWI
FGDVWISESS EEGGKTKHRP AGFEEKGEIV ITKPYPYLAR YIWGDETNFG QPEWKGDADR
YVDTYWGKWD GVWAYTQGDF AMKYEDESFS LHGRSDDVIN VSGHRMGTEE IEGAILRDKQ
INPDSPVGNA IVIGAPHREK GLTPVAFIQT VPGAKLTLED QRRLSELVRQ EKGVVAVPSD
YIEVLQFPET RSGKYMRRFL SNLLNGEELG DTSTLRNPES IDEIRPKIEQ WRMKTKMEEE
QKIFEIYRFF RVQYNDVLPG QRVATVTITN PPVNALNERA LDELNTIVSH LERRDEIKVV
IFTGQGTGSF VAGADVKQFL EEMFDVQDVL PLANKAHMAF SKIEKLGKPV IAAVNGVALG
GGNEFQMATH YRIAEPHAEF GQPEINLNLI PGYGGTQRLP RLLQDRRGTD GFLKALEIIL
NGRKIDVEEA KQIGLIDEII QESDDVLVRA AALAREYILR GTGALKEAFD RHNSLVQQWN
TPQAFPQEAI DNSAEIQRIL RQSKWAGREQ AANRALEATR IGYEQGIKKG MEREAQLFAE
AVIDPNGGKS GIQAFLDKKS MPLPTRPRFQ PTEEKQDELI EQGELLPIGA PYFPGFTPIP
EWQYAYAVVK NDETGAVDHG DPIDAEKKIV IPVEKPTANE VLLYVLASEV NFNDIWALTG
IPVSTLDDHD LDYHVTGSGG IALVASVGPE VKREGRVKVG DLVTIYSGQN NLLSPTVGLD
PMFADFSIQG YQGPDGSHQQ FMIAQAPQVH VKPQDATLEA AGSYILNLGT IYRALFTTLS
IEPNKTMFVE GAATGTGLEA LKSAARNGLA VTGMVSSEER AAYIQEQGAA GVINRRNPEY
GNAFTKVPAD PSQWAAWEAA GQKILDDYRA QNNGRLADYV VSHAGEVAFP RSFQMMEKNG
VLTFYGASSG YHFTFMGKEG ASTPRDMYEK ALLRAGESVL IYYGTDTKED GIVDQTGLVA
IEAARDMGAR IVVATYTDAQ KEFVQSLGYG DAVRGVLSIE EIKRREGENF VWPDTMPDFP
NPKTETEAFK EAVRYFTDYI FKPFGGAVAK YLRSPDNPRG YPDLIFDRAG HDALGVSTTL
LKPYTGRVVF SEDMNARRYS FYAPQVWMRQ RRVYMPTANI WGTHLSNAYE VIRMNEMIDA
GMLEITEPVF VEFDQLPEAH QEMWENRHVG SSYVVNHAIP QTGLKTKDQL YEAWSAQMNE
KTSE
//