ID A0A0N0K3N7_9PROT Unreviewed; 1835 AA.
AC A0A0N0K3N7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-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=IP88_02760 {ECO:0000313|EMBL:KPF78935.1};
OS alpha proteobacterium AAP81b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF78935.1, ECO:0000313|Proteomes:UP000037971};
RN [1] {ECO:0000313|EMBL:KPF78935.1, ECO:0000313|Proteomes:UP000037971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP81b {ECO:0000313|EMBL:KPF78935.1,
RC ECO:0000313|Proteomes:UP000037971};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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:KPF78935.1}.
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DR EMBL; LJHX01000024; KPF78935.1; -; Genomic_DNA.
DR STRING; 1523432.IP88_02760; -.
DR PATRIC; fig|1523432.3.peg.1679; -.
DR Proteomes; UP000037971; 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; 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; 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; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00378; ECH_1; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037971}.
FT DOMAIN 158..246
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 381..655
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 753..821
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 1835 AA; 197137 MW; BA914CFF416A2FC0 CRC64;
MTLQTLSPPR TAAAAAVVAD VNPVGNRAAW EAMRAATIAD PGVFHGGIAA RNLHWRVELP
TGAAAWLSFN GSAWTGWDAD TLEPVVADLP AGFVPWDRAF NPDDAPHFRW FEGGRTNCCF
NEQDRHVLAG GGAEIAVIFE GDRWDLAADN GRGAPVDCVH VTRRQLLLET AKCAVALQRL
GLKAGDRIAI NMPNVLGQLF WTEAAKRIGV LYTPVFGGFS DKTLSDRIHD AGARVVITAD
GGYRMAQVSA FKTAYTDPAL DNYVPVSVAL DLLRERVGGA DLGLAADIAA QIADTVTETL
KGEVTVERGD VMRGVGRALA DLGKAGTVDA GLAARIRIAV AEALVATPPR VEAVIVVAHA
HLPDIVWRDR DVWSHELTDA ALVEILAAAG LASEAELLAL DDQAFVRALW HAAPPLAVDA
EFPMFFIYTS GSTGKPKGVV HVHGGYAAGI METMKIAFDA RPGDTLYVVA DPGWITGQSY
MIAAPLLCRV TTLIGEGAPV FPHAGRFAAM IERHNVTIFK AGVTFLKSVM SDPQNLKDIE
VYDLSRLRVA TFCAEPCSPS VQAFGMEHVT PWYINSYWAT EHGGIAWTHF YGNGDFPLAA
DARTFPLPWI LGDVWVEDAE GQGGAVAPLA RSATDGVNWR RAEEGEKGEI VIAAPYPYLA
RTVWGDAGNF AVADGKVVGG WKGDSGRWAS GYWHRWQGVW AYTQGDFAVR HADEGFSLHG
RSDDVINVSG HRMGTEEIEG AILRDKQLDP DSPVGNVLVV GAPHREKGLT PIAFVTAAPG
QTLTRDDFRR LSDLVRQEKG AVAVPGDFIQ VSQFPETRSG KYMRRMVRAL VEGGELGDVT
TLRNPESLDE IRAAIGQWQK KQQLSEDQQI FDRYRYFRIQ YNDVAPGKKV ATVFVTNPPV
NALNERAIDE LVIVVEHLSR RDDVVAVVFT GDGTASFVAG ADIRQFLDEI HTIEEARVLP
ANAQLAFGKI EAMNKPCVAA IQGVALGGGM EFALACHWRV AEAHARFGQP EIRLRLLPGY
GGTQRLPRLL ADKHGPDGLL HALDLILGGR SIDGEAAVGI GLVETLASGS DDALSLAHAA
VREFVRHGET SALGRTWAAR RKAAKQEWQA ASHIDLDAAL ADDFVQRMLR QLDWAGRGPA
GARAIDAIRT GWTQGMAAGL AREAELFAEA VIDPQGGKTG IRLFMDKKAP PLPVRRDGVY
IDSEHAARGE RLEAAGDLLP VGAPFFPGVS AIPGHQYAFG IARDAETGAP RFGQPAAHEK
ELIVPVPTPE PNEALVYLLT SEVNFNDIWA LTGIPVSPFD GHEEDVQVTG SGGLALVAAL
GSEVRGEGRL KVGDMVAVYS GTSDLLSPMA GRDPMYADFA IQGYETKTGS HAQFLTVQAP
QLHAVPGDLT LEQAGSYILN LGTIVRCLFT TLEIVGGKTI FIEGSATGTG LDALKTAKAS
GLAVTGLVSS PARAAFVATK GAVGALDRTD PRFAALFTAV PDGDPAAWAA WEKAGGPLLD
EYRRLNGGKL ADYAVSHAGE TAFPRSFQLL ADGGKLAFYG ASSGYHLSFM GKAGSATPEA
MLARAGARGG EAVLIFYGPH SRDLADPMGL EMIEAARAIG ARTVVVTTTD GQREFILSLG
FEDAVAGVVS LEAIKRREGG NFDWPDTMPR LPVARDDIER FRDAVRDFQD KTLKPFGNAI
GKLLRSPDNP RGNPDIVLER AGQDTLGVTT ALVKPFTGRI VYAEDMTGRR YNFYAPQVWT
RQRRIVMPSA EIRGTHLCNA YEVTRMNDMV AAGLLDVTEP TMVPWEGLPE AHQAMWDNRH
SGATYVVNHA LPAPGLRSKD ELFEAWAAQT AKTEA
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