ID A0A1I2P1G3_9BACT Unreviewed; 696 AA.
AC A0A1I2P1G3;
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=SAMN04487988_101407 {ECO:0000313|EMBL:SFG09992.1};
OS Algoriphagus hitonicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=435880 {ECO:0000313|EMBL:SFG09992.1, ECO:0000313|Proteomes:UP000199642};
RN [1] {ECO:0000313|EMBL:SFG09992.1, ECO:0000313|Proteomes:UP000199642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19315 {ECO:0000313|EMBL:SFG09992.1,
RC ECO:0000313|Proteomes:UP000199642};
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}.
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DR EMBL; FOPC01000001; SFG09992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2P1G3; -.
DR STRING; 435880.SAMN04487988_101407; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000199642; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 214..326
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 371..690
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 696 AA; 76668 MW; EADC80B9D8BBEB61 CRC64;
MTNAIYLTTT EPFSGKSIFA LGLMHMLASK TDKLAYFKPI ISGIKKNKDR RLDLLAKQFN
LSQSYEEMYA FTRKNALKEI NKRNEAFLID TIIEKFNSLR ENADFVVVEG TDFTDINTNV
EFDGNVSIAK NLGIPAAIIL NAAGRTTSEI IDLALASTNS YLSRGVQVLT LIANKVEQGK
LEEVLRRLRF VLPASILINA IPSHEQLSNP TMGEIMDSLN AKLLFGGQFL TNRVDHSIVG
AMQLHNFLAR LSNNTLVVTP GDRGDILVGS LQANISRNFG KVAGVIVSGG MLPEGTIVKL
IEGLETVVPV LQVEDGTFMV VTKVNQIRAR IAPEDTEKIA LAIKLFEDYV DEKALEERII
SFSSDIMTPR MFQYQIVRRA KSHKKHIVLP EGNDERILKA ADMLIRQDVV DLTLLGNREE
IHNMVAKLNL SMDLDKVQIE DPASSIRFDD YAQTLYELRK NKGLTLEVAR DLMMDVSYFG
TMMVHKKHAD GMVSGAVHTT QHTIRPALQF VKTKPGVNTV SSVFFMCLPN RVSVFGDCAV
VPNPSSEQLA DIAISSAESA MMFGIEPKIA MLSYSSGTSG AGEEVEKVRK ATQIVKERRP
ELKIEGPIQY DAAVDPIVGM QKLPNSEVAG QASVLIFPDL NTGNNTYKAV QRETGAIAIG
PMLQGLNKPV NDLSRGCTVI DVFNTVVITA IQAQEF
//
