GenomeNet

Database: UniProt/TrEMBL
Entry: E3HM28_ACHXA
LinkDB: E3HM28_ACHXA
Original site: E3HM28_ACHXA 
ID   E3HM28_ACHXA            Unreviewed;       540 AA.
AC   E3HM28;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=AMP-binding enzyme family protein 9 {ECO:0000313|EMBL:ADP15730.1};
GN   OrderedLocusNames=AXYL_02409 {ECO:0000313|EMBL:ADP15730.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP15730.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP15730.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP15730.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002287; ADP15730.1; -; Genomic_DNA.
DR   RefSeq; WP_013393050.1; NC_014640.1.
DR   AlphaFoldDB; E3HM28; -.
DR   STRING; 762376.AXYL_02409; -.
DR   KEGG; axy:AXYL_02409; -.
DR   PATRIC; fig|762376.5.peg.2404; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_4; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000006876; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   CDD; cd05971; MACS_like_3; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR049515; MACS_put.
DR   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 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   Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT   DOMAIN          38..400
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          451..528
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   540 AA;  58197 MW;  F0161397BD68F721 CRC64;
     MLSRADSYTQ LASQFQWQVP AAYNIGVDAC DKWADGSGRL ALIYEKSDGA QSRYTFDQIK
     ALSNRLAHSL ERHGVKRGDR VAVYLPQAPE TAVTHIAVYK MGAVAVPLFT LFGVDAIQYR
     LANSGAAALV TDAEGCRKLR EIRASLPDLK VVYCIDPDCP DDAVPFHAAL AAESDDYTPA
     ATAADDPAVI IYTSGTTGKP KGALHAHRVL LGHLPGVEMS HEFFPENAAL MWTPADWAWI
     GGLLDVLLPS WHHGVPVLAR RFEKFDGASA FELMARHGVT HTFLPPTALK MMRGTELPAG
     AGALALRSVA SGGESLGAEL IDWGRRVLGV TINEFYGQTE CNMLVSSCSS LFDPCIGAIG
     RAAPGHRVAI VDDSGVEVAD GQEGNIGVLR PDPVMFLGYW NNPEATAEKF AGDYLLTGDQ
     GVRDAEGFIR FVGRNDDVIT SAGYRIGPGP IEDCLIGHPA VRMAAVVGVP DAQRTEIVMA
     YVVLNEGYEG NDALVKDLQA HVRKRLAAHE YPRAIRFVTS LPTTATGKII RRELRDGSYS
//
DBGET integrated database retrieval system