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Database: UniProt
Entry: A7HUW5_PARL1
LinkDB: A7HUW5_PARL1
Original site: A7HUW5_PARL1 
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
//
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