ID A0A1H1V516_9CELL Unreviewed; 700 AA.
AC A0A1H1V516;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04489860_2394 {ECO:0000313|EMBL:SDS79793.1};
OS Paraoerskovia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Paraoerskovia.
OX NCBI_TaxID=545619 {ECO:0000313|EMBL:SDS79793.1, ECO:0000313|Proteomes:UP000185663};
RN [1] {ECO:0000313|EMBL:SDS79793.1, ECO:0000313|Proteomes:UP000185663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22126 {ECO:0000313|EMBL:SDS79793.1,
RC ECO:0000313|Proteomes:UP000185663};
RA de Groot N.N.;
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}.
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; LT629776; SDS79793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1V516; -.
DR STRING; 545619.SAMN04489860_2394; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000185663; Chromosome i.
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 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; 2.
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:UP000185663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 214..325
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 370..687
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 700 AA; 74261 MW; FC7ABD234C6C4E85 CRC64;
MNTRSVYITS PEGDTGKSTV ALGVLDQLVR RATRVGVFRP VARNTARGDA AEDRDYVLEL
LLAHDGVDLA YEDAIGVTYE DVHADPDAAL SRILSRYHAV AAVCDVVVVI GTDYTDIAGP
TELAFNARVA ANLGSPVLLV VSGRNRDAGG IRQLAEVSVG ELQANHAQPV GVIANRCTPT
DLETVRSELD ALDLPSWAIP DEPFLTAPTV QAMMEAVDGR LVFGDRELLG REVLDVLVGA
MSLEHLLERI TDGALIITPG DRAELLIGLI AAHSAPGFPS IAGIVLNGGF YPPPTSADLI
ADLDPRLPVI RTEMGTFRTA SAASRVRGRV TKDSQRKIDT ALALFEQNVD GATLLQHLDV
PRPDTVTPLM FEYELLSRAR ADRKRIVLPE GSDDRILRAA STLLGRQVAD LVILGEEPEV
RSRAIELGLN IEAARILSPH DPAYVDRFAA EYTRLRAHKG MTVERAREIV TDVSYFGTMM
VHMGDADGMV SGAAHTTAHT IRPSFEIIKT VPGVSVVSSV FLMCLEDRVL VYGDCAVNPD
PSATELADIA ISSAATAAQF GVNPKVAMLS YSTGASGSGA DVEKVRDATA LVRERSTDLF
VEGPIQYDAA VDASVAASKM PGSDVAGKAT VFIFPDLNTG NNTYKAVQRS AGAVAVGPVL
QGLNKPVNDL SRGALVQDIV NTVAITAIQA QAGTSQGDPA
//
