ID A7HUW5_PARL1 Unreviewed; 632 AA.
AC A7HUW5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ABS63698.1};
GN OrderedLocusNames=Plav_2084 {ECO:0000313|EMBL:ABS63698.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS63698.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS63698.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP000774; ABS63698.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HUW5; -.
DR STRING; 402881.Plav_2084; -.
DR KEGG; pla:Plav_2084; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_5_5; -.
DR Proteomes; UP000006377; 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Ligase {ECO:0000313|EMBL:ABS63698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377}.
FT DOMAIN 4..57
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 64..448
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 514..592
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 632 AA; 69268 MW; 8796643F7CC42745 CRC64;
MGRYKDTYDA WKRDPEGFWA EAAKEIDWFK PADKILEEKN GLSRWFVGAE TNSCWNALDR
HVKAGHGDRT ALIYDSAMLG RVKKFTYAEL LDKVATFAGV LQSHGITKGD RVLIYMPMVP
QAAVAMLACA RLGAIHSVVF GGFAAKELAT RIDDAKPKLI VSASCGLEPG RVIAYKPLMD
KAIEMSAHKP AACIVLQREM EEAPLIPGRD FDWKAEMDKA AAANNKPDCV SVAATDPLYV
LYTSGTTGKP KGVVRDNGGH MVALKWSMKN VYDIDPGDTF WAASDVGWVV GHSYIVYAPL
FHGCTTILFE GKPVGTPDAG TYWRIIAEHG VKALFTAPTA FRAIRKEDPK AELVGKYDLT
KFEVLYLAGE RADPDTIQWA EQALQRPVID HWWQTESGWP MVSNPMGIER LPVKHGSPSV
PLPGYEIHVV DEACKQVGPN TTGAIVVKLP LPPGCLPTLW ENEAGFRESY LADYPGYYKT
ADAGFLDEDG YLYVMSRTDD IINVAGHRLS TGGMEEVLAA HPDVAECAVI GIADAMKGQV
PVGFLVLNAG VARPAAEIEQ EAVQLIRERI GPVASFRKAM VVQRLPKTRS GKVLRGTMRK
IADGAEWTTP ATIDDPAILD EIKTVLEREL AR
//