ID A0A1B2R563_9BORD Unreviewed; 552 AA.
AC A0A1B2R563;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Poly(3-hydroxyalkanoate) polymerase {ECO:0000313|EMBL:AOB32112.1};
GN ORFNames=AKI39_17420 {ECO:0000313|EMBL:AOB32112.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB32112.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP012334; AOB32112.1; -; Genomic_DNA.
DR RefSeq; WP_066638797.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R563; -.
DR STRING; 1697043.AKI39_17420; -.
DR KEGG; boh:AKI39_17420; -.
DR PATRIC; fig|1697043.4.peg.3578; -.
DR OrthoDB; 7208816at2; -.
DR Proteomes; UP000093512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010963; PHA_synth_I.
DR InterPro; IPR010941; PhaC_N.
DR NCBIfam; TIGR01838; PHA_synth_I; 1.
DR PANTHER; PTHR36837; POLY(3-HYDROXYALKANOATE) POLYMERASE SUBUNIT PHAC; 1.
DR PANTHER; PTHR36837:SF2; POLY(3-HYDROXYALKANOATE) POLYMERASE SUBUNIT PHAC; 1.
DR Pfam; PF07167; PhaC_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000093512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..213
FT /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07167"
FT REGION 521..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 60469 MW; B28E546583E79204 CRC64;
MTAHPSAAWP VPVGVAPDIL AQIQADFSRD WQRLADDARA GRLEPPSDKR FAGEAWRRSP
HHLVMAHAYL LSARALHRMV DAASVSEALR DRLRFSIMQW LDAIAPSNFL AFNPDAQESV
LASAGKALNE GLANLLNDLG KGRITQTDES QFEIGVNVAV TPGQVVFENP LFQLIQYTPS
TPTVYQRPLV IVPPNINKFY VLDLQPANSF VRHAVEAGFT VFMMSWRNPV PADEDGVDRA
QWDDYLENAV LPALRMAGEI TGQPQVNALG FCVGGTLLAS ALALAHARGE RPVAALTLLT
ALLDFRDTGV LSVFVDETHA LLRDRLLGGG GLMPGRELAT TFSFLRPNEL VWNYVVDNYL
KGRKPPAFDL LFWNADSTNL PGPFFAWYFR NTYLENNLKV PGRCVVADVP LDLTSLDMPA
YIFGSREDHI VPWTSAYAST QLLRGTQRFV LGASGHIAGV INPPAKKRRS YWTTAAGNGN
GNGDGNGNAM LPGDPSAWLA RAEEHPGSWW PDWTAWLAGH SGRQGKAPSR MGSAEHPPIE
PAPGRYVKVR AM
//