ID A0A1I6NTM3_9FLAO Unreviewed; 697 AA.
AC A0A1I6NTM3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphate acetyltransferase {ECO:0000256|ARBA:ARBA00021528, ECO:0000256|PIRNR:PIRNR006107};
DE EC=2.3.1.8 {ECO:0000256|ARBA:ARBA00012707, ECO:0000256|PIRNR:PIRNR006107};
DE AltName: Full=Phosphotransacetylase {ECO:0000256|ARBA:ARBA00031108, ECO:0000256|PIRNR:PIRNR006107};
GN ORFNames=SAMN04488006_0544 {ECO:0000313|EMBL:SFS31225.1};
OS Lutibacter maritimus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=593133 {ECO:0000313|EMBL:SFS31225.1, ECO:0000313|Proteomes:UP000199312};
RN [1] {ECO:0000313|Proteomes:UP000199312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24450 {ECO:0000313|Proteomes:UP000199312};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in acetate metabolism.
CC {ECO:0000256|PIRNR:PIRNR006107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC Evidence={ECO:0000256|PIRNR:PIRNR006107};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2. {ECO:0000256|ARBA:ARBA00004989,
CC ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006107}.
CC -!- DOMAIN: The N-terminal region seems to be important for proper
CC quaternary structure. The C-terminal region contains the substrate-
CC binding site. {ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family.
CC {ECO:0000256|ARBA:ARBA00008756, ECO:0000256|PIRNR:PIRNR006107}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC {ECO:0000256|ARBA:ARBA00009786, ECO:0000256|PIRNR:PIRNR006107}.
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DR EMBL; FOZP01000001; SFS31225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6NTM3; -.
DR STRING; 593133.SAMN04488006_0544; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000199312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03109; DTBS; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR016475; P-Actrans_bac.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR NCBIfam; TIGR00651; pta; 1.
DR PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR006107};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR006107};
KW Reference proteome {ECO:0000313|Proteomes:UP000199312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 215..326
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 372..691
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 697 AA; 76303 MW; 1782171F77D44281 CRC64;
MNKAIYIATS EANSGKSIVA LGLMRMLLGK TAKVGYFRPI IDGHKGGKKD NHINTIISHF
ELDINPNEAF AFTRAEFISK RNQGKEGEIY DTIIEKYKEI EEKNDFVLVE GTDFSGEGTA
IELDANILIA KNLGIPAIIV SSGIGKTLDE FINGLHIAYD SFAEKEVKVL AVIANKVQEK
NIEIVREGVE KNLPKDVSVN VIPLIPSLQN PTIKEIAKAI DAKVIFGKEY LNNQTTTFKV
GAMQLRNYLT HLEQDCLIIT PGDRADIILG ALQANISSNY PSISGIVLTG GILPEEPIVK
LIDGLQHIVP ILSVNEGTFD VANKIGAVRS HMYAENKEKI ITSLNTFDKY CDADKLTEKF
ETFKNNGITP RMFQYNLLKR AKTSRKHIVL PEGNDDRIIA AAVRLIQMDI VDITILGDKN
KIEETLLRLG LKMDFDKVSI INPLDSSYYN DFVNTFYELR KAKGVTKEIA EDLMSDVSYF
GTMMVYKGLA DGMVSGAAHT TQHTIKPALQ FVKTKPGVSV VSSVFFMCLD DRVSVFGDCA
INPNPTAEQL AEIAISSAES SINFGIEPKI AMLSYSSGAS GKGEDVDIVR KATEIVKEKR
PDLKVEGPIQ YDAAVDPSVG KSKMPNSEVA GQANVLIFPD LNTGNNTYKA VQRETGALAI
GPMLQGLNKP VNDLSRGCTI DDIFNTVILT AIQAQGL
//
