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Database: UniProt
Entry: A0A1H7NRE5_9GAMM
LinkDB: A0A1H7NRE5_9GAMM
Original site: A0A1H7NRE5_9GAMM 
ID   A0A1H7NRE5_9GAMM        Unreviewed;       703 AA.
AC   A0A1H7NRE5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN05216262_10863 {ECO:0000313|EMBL:SEL25986.1};
OS   Colwellia chukchiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL25986.1, ECO:0000313|Proteomes:UP000199297};
RN   [1] {ECO:0000313|Proteomes:UP000199297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
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   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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; FOBI01000008; SEL25986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7NRE5; -.
DR   STRING; 641665.GCA_002104455_03541; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000199297; 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:UP000199297};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          225..334
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          383..698
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   703 AA;  76442 MW;  BE3B385ACD6FB39D CRC64;
     MAHRIMLIPA GFGVGLSSIS LGLIHACQQQ GINTGHFKPI SQPARNCRNK ASAQAKANEN
     SSSIALSYVE QQIGDGRSDI VLEQIIENFN AIDKAHDVVI IEGLIPTTRQ PYAGRVNRDV
     ARALSAEIVL VAAQDNDSLD EFEDRIEMSA ETFGGIKNPK LIGCIINKIN APDSHEFGLL
     PREQEFNTAL DIAPLTKLSI FKSQHFNLLG AVPWEMDLIA PRVVDIAHYL NAEIINAGDM
     DHRRVRSISF CARSVDNLMS HLQPSRLIVT PGDRTDIIIA TCLSALNGTK VAALVLTNGY
     IPNESIQSLC QQALDVGLPV LSVPWDTWQT SRHLINFTPD IPQDDVQRQE KVKEYVAEHL
     TPNWLLQLGN QAPISEKMSP PAFRHKLTEL ARQANKLIIL PEGTDVRTIK AAAICVERNI
     ARCQLLGDKD TILRIAQQQG IHLPDGLLIT DPRTIRENYV APMVQLRKAK GMTEVVAKQQ
     LKEDIVLATM MLQLGQVDGL VSGAVNTTAH TIRPALSLIK TAEGSALVSS IFFMLLPDQV
     LIYGDCAINP EPNAEQLADI AIQSADSAIQ FGIAPKVAMI SYSTGTSGFG ADVEKVAAAT
     KIAQQRRPDL VIDGPLQYDA AIMENVARKK APNSPVAGQA NVFIFPDLNT GNTTYKAVQR
     SADLVSIGPM LQGMRKPVND LSRGALVDDI VYTIALTAIQ AQA
//
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