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Database: UniProt
Entry: L0GUG5_9GAMM
LinkDB: L0GUG5_9GAMM
Original site: L0GUG5_9GAMM 
ID   L0GUG5_9GAMM            Unreviewed;       357 AA.
AC   L0GUG5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Poly(3-hydroxyalkanoate) polymerase subunit PhaC {ECO:0000256|ARBA:ARBA00019065};
DE   AltName: Full=PHB synthase subunit PhaC {ECO:0000256|ARBA:ARBA00033356};
GN   ORFNames=Thimo_1640 {ECO:0000313|EMBL:AGA90418.1};
OS   Thioflavicoccus mobilis 8321.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thioflavicoccus.
OX   NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA90418.1, ECO:0000313|Proteomes:UP000010816};
RN   [1] {ECO:0000313|EMBL:AGA90418.1, ECO:0000313|Proteomes:UP000010816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8321 {ECO:0000313|EMBL:AGA90418.1,
RC   ECO:0000313|Proteomes:UP000010816};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA   Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004683}.
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DR   EMBL; CP003051; AGA90418.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0GUG5; -.
DR   STRING; 765912.Thimo_1640; -.
DR   KEGG; tmb:Thimo_1640; -.
DR   PATRIC; fig|765912.4.peg.1612; -.
DR   eggNOG; COG3243; Bacteria.
DR   HOGENOM; CLU_035017_0_0_6; -.
DR   UniPathway; UPA00917; -.
DR   Proteomes; UP000010816; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010125; PHA_synth_III_C.
DR   NCBIfam; TIGR01836; PHA_synth_III_C; 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   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   PHB biosynthesis {ECO:0000256|ARBA:ARBA00022752};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010816}.
FT   DOMAIN          70..336
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   357 AA;  40235 MW;  6F2BAAE9E2FB3CF5 CRC64;
     MSVFPIEIRP DKLTEEMLAY SRKLSEGMQN LLNADEIDTG VTPKDAVYRE DKLVLYRYQR
     PAQVVTQPIP LLIVYALVNR PYMTDLQEDR STIKGLLATG QDVYLIDWGY PDQSDRALTL
     DDYINGYIDR CVDYLRETHG VDQVNILGIC QGGTFSLCYT ALHPEKVKNL VTMVTPVDFQ
     TPGNLLSAWV QNVDVDLAVD TMGNIPGELL NWTFLSLKPF SLTGQKYVNM VDLLDDEAKV
     KNFLRMEQWI FDSPDQAGEA FRQFIKDFYQ RNVLINGGLV IGDRAIDLRN IRCPILNIYA
     MQDHLVPPDG SKALDGLTAS EDYTELAFPG GHIGIYVSGK AQKQVTPAIG NWLNERA
//
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