ID A8LRC0_DINSH Unreviewed; 630 AA.
AC A8LRC0;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ABV92570.1};
DE EC=6.2.1.- {ECO:0000313|EMBL:ABV92570.1};
GN OrderedLocusNames=Dshi_0825 {ECO:0000313|EMBL:ABV92570.1};
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV92570.1, ECO:0000313|Proteomes:UP000006833};
RN [1] {ECO:0000313|Proteomes:UP000006833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC {ECO:0000313|Proteomes:UP000006833};
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
RN [2] {ECO:0007829|PDB:5GXD}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH AMP AND COA.
RA Zhang Y.Z., Wang P., Cao H.Y.;
RT "Structure of acryloyl-CoA lyase PrpE from Dinoroseobacter shibae DFL 12.";
RL Submitted (SEP-2016) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP000830; ABV92570.1; -; Genomic_DNA.
DR RefSeq; WP_012177503.1; NC_009952.1.
DR PDB; 5GXD; X-ray; 2.00 A; A=1-630.
DR PDBsum; 5GXD; -.
DR AlphaFoldDB; A8LRC0; -.
DR SMR; A8LRC0; -.
DR STRING; 398580.Dshi_0825; -.
DR KEGG; dsh:Dshi_0825; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_5_5; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000006833; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05967; PrpE; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5GXD};
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Ligase {ECO:0000313|EMBL:ABV92570.1};
KW Nucleotide-binding {ECO:0007829|PDB:5GXD};
KW Reference proteome {ECO:0000313|Proteomes:UP000006833}.
FT DOMAIN 3..57
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 63..445
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 510..588
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 168
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 171
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 281
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 308
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 365
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 386
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 387
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 390
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 391
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 478
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 493
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 499
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 504
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 533
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 563
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
FT BINDING 573
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0007829|PDB:5GXD"
SQ SEQUENCE 630 AA; 68415 MW; 0A44C974DE2441ED CRC64;
MTYSQTYAAW KNDPEGFWME AAQAIDWVTP PGAALNSDNA PLYEWFTDAE VNTCFNAVDR
HVQAGNGDRV AIIHDSPVTH TKQEITYAEL QERVSLLAGA LRAKGIEKGD RVLIYMPMVP
QALEAMLACA RLGAIHSVVF GGFAANELAV RIDDATPKAI IAASCGIEPG RVVHYKPLLD
GAIDLATHKP DFCLIFQREQ EVAHLEPGRD FDWHEAQYGV DPAECVPVAG NHPAYILYTS
GTTGQPKGVL RPTAGHLVAL NWTMKNIYNV DPGDVFWAAS DVGWVVGHSY ICYAPLIHGN
TTIVFEGKPV GTPDAGTFWR VISEHKVKSF FTAPTALRAV KREDPNGEFI GKYDLSHLKT
VYLAGERADP DTIQWTMDKL GVPVIDHWWQ TETGWAIAAN PMGIEHLPVK IGSPSVAMPG
YDVQVLDEGG HPVAPGTLGA IAVKLPLAPG TLPNLWQAEE RFVKSYLTTF PGYYETGDAG
YIDEDGYLYI MARTDDVINV AGHRLSTGAM EEVLASHPDV AECAVIGVSD TLKGQMPLGF
LCLSAGVNRP HDEIAKECVK LVREKIGPVA AFKLACVVDR LPKTRSGKIL RGTMVNIADG
TPWKMPATID DPAILDEITE ALGKLGYPAS
//
