ID Q1GVU6_SPHAL Unreviewed; 590 AA.
AC Q1GVU6;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Poly(R)-hydroxyalkanoic acid synthase, class I {ECO:0000313|EMBL:ABF52226.1};
GN OrderedLocusNames=Sala_0505 {ECO:0000313|EMBL:ABF52226.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF52226.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF52226.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP000356; ABF52226.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1GVU6; -.
DR STRING; 317655.Sala_0505; -.
DR ESTHER; sphal-q1gvu6; PHA_synth_I.
DR KEGG; sal:Sala_0505; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_017387_1_0_5; -.
DR OrthoDB; 7208816at2; -.
DR Proteomes; UP000006578; 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; IPR000073; AB_hydrolase_1.
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; PF00561; Abhydrolase_1; 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:UP000006578};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 103..271
FT /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07167"
FT DOMAIN 273..514
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65312 MW; 6E02B5E433C7E5A8 CRC64;
MTDMGEDKSS GAANPFMPSP DDVQHWTSVM GRAQQMMLDY VLGQANQRNS AAANLFDPAS
WLQNPTTQLW AEQSTKMWEQ GAAFWASLAT LQPSLTPDAD ARQDKRFADP DWTTNPVFAL
IRQTYGLLAE QLLATTRNMQ GIDEQARAKL EFAAKNMAEA LSPSNLAITN PEVIKRAVET
RGESLLKGLG HMLSDLSRGQ LSHVDPDAFE VGVNIATTPG KVIHETDLYQ LIQYDPATKD
VFAVPLVIFP PWINRFYILD LNPQKSFVKW ATEQGLTVFM VSWKSADASM SEIVWDDYVS
AQVDAIDTVR DLLDVPHVHT IGYCVAGTTL AATLAMLAAR GEADGVKSAT FLTAQVDFEL
AGDLKLFVDD AYLALLQQLS APGYLDGRYM AATFNSLRGR DLIWNYVVNN YLLGNDYPPF
DLLYWNGDTT NLPAKWHRQY LTELYRDNRM VIPNSLSVCG TPIDLRKIAT PAYIQAGRED
HIAPAASVWR MMHHLSGPRT FLLAGSGHIA GVVNPPAAGK YQYWTGDNDA VTLDDFIAGA
TETKGSWWPH WAGWIAAQDD KKVPAKGARI PGKGRRKAIE DAPGRYVKQR
//
