ID C4ZIY7_THASP Unreviewed; 607 AA.
AC C4ZIY7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Poly(R)-hydroxyalkanoic acid synthase, class I {ECO:0000313|EMBL:ACK53500.1};
GN OrderedLocusNames=Tmz1t_0728 {ECO:0000313|EMBL:ACK53500.1};
OS Thauera aminoaromatica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=164330 {ECO:0000313|EMBL:ACK53500.1, ECO:0000313|Proteomes:UP000002186};
RN [1] {ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK53500.1, ECO:0000313|Proteomes:UP000002186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ1T {ECO:0000313|EMBL:ACK53500.1,
RC ECO:0000313|Proteomes:UP000002186};
RX PubMed=23407619; DOI=10.4056/sigs.2696029;
RA Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL Stand. Genomic Sci. 6:325-335(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP001281; ACK53500.1; -; Genomic_DNA.
DR RefSeq; WP_004312074.1; NC_011662.2.
DR AlphaFoldDB; C4ZIY7; -.
DR STRING; 85643.Tmz1t_0728; -.
DR KEGG; tmz:Tmz1t_0728; -.
DR eggNOG; COG3243; Bacteria.
DR HOGENOM; CLU_017387_1_0_4; -.
DR OrthoDB; 7208816at2; -.
DR Proteomes; UP000002186; 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:UP000002186};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..281
FT /note="Poly-beta-hydroxybutyrate polymerase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07167"
FT DOMAIN 283..526
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 607 AA; 68029 MW; 4263666033ABB924 CRC64;
MAAPSNETPA CDLPDPQEVA KTYAEVARRA SHLISDHVHR QLKKGVSTPA DELGIAQAFM
DMMAKLLANP YKLAQAQMNL VWDYFSLWQH SMMRVAGLSA SPVAAPEKSD KRFKDEEWEQ
HFLFDFIKQS YLIAARHIHD TVSGVDGLDE QTQKKVTFYT RQYIDALSPS NFAMTNPEVF
RETVKSHGQN LLKGLNNLLR DVEDGGGNLR VKMTDTSAFE LGKNVATTPG KVVFQTEMMQ
LLQYTPSTEK VLKKPLLIVP PWINKFYILD LREKNSYIKW AVDQGHTVFV ISWVNPDERL
AQKSFDAYVK EGVIAALDAI ERQTGEKEVN AAGYCLGGTL LATTLAYLAA KRQKRILSAT
FFTTMTDFTD PGELGVFIDE GQVSSLEKKM FERGYLEGSE MAGTFNMLRA NDLIWSFVVN
NYLLGKDPFP FDLLYWNSDS TRMPAAMHSF YLRTMYMENR LIEPGGIEID GTPIDLGKIK
VPCYFISTIE DHIAPWKSTY MGARRFGGPT RFVLGGSGHI AGIVNPPAAN KYGYWLNPSA
KLAETADAWL EGAQQHPGSW WTDWQAWVTA HDSEQTEARD PVNGKLEVLE DAPGSFVKIR
IDAKAAA
//
