ID A0A098LPA4_9FLAO Unreviewed; 696 AA.
AC A0A098LPA4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=JCM19538_2561 {ECO:0000313|EMBL:GAL88198.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL88198.1, ECO:0000313|Proteomes:UP000030184};
RN [1] {ECO:0000313|EMBL:GAL88198.1, ECO:0000313|Proteomes:UP000030184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19538 {ECO:0000313|EMBL:GAL88198.1,
RC ECO:0000313|Proteomes:UP000030184};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAL88198.1}.
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DR EMBL; BBNY01000001; GAL88198.1; -; Genomic_DNA.
DR RefSeq; WP_045371093.1; NZ_BBNY01000001.1.
DR AlphaFoldDB; A0A098LPA4; -.
DR OrthoDB; 9805787at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000030184; 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..325
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; 76558 MW; A23108E7C0D4FE3E CRC64;
MSKGIYVATI EPNSGKSVVV LGLMRMLLGK TAKVGYFRPI IEDTKNGEPD NHINTVVSYF
ELDINYKKTF AYKRSEVLEL YNKGKSGDVI DHVIKRYKYL EERFDIVLVE GTDFSHENSS
LELDINMLIS KNLGLPVIIV SRGDGLNVSE IADNVQIAHD TFKEEVDVLS IMTNKVKPED
TSKLKALLQT RITSGTDITV IPKVKSLASP TIKEIVKKLE GNILFGEDLI NNQSENFSVG
AMQLRNYLTH LKENALVITP GDRADIILGA LQANISKNYP KISGIVLTGG LIPEDPILKL
IEGLSSVVPI ISVKQGTFAV TNIIGKIRSK IYAENTEKIE TSIATFEKHV DTDKLSDDLI
TFQSDIFTPR MFQYNLLQRA LSNKKHIVLP EGTDERVLRA AARLIDAQVV DLTLIGDESI
IKEQIEKLDI PLDTTHINIV SPLKSPHFED YANTFYELRK HKNVNLDMAK DAMADVSYFA
TMMIYKGHAD GMVSGAVHTT AHTLRPALQF IKTKPGVNIV SSVFFMCLED RVSVFGDCAI
NPNPNAEQLA EIAISSAKTA RDFGIEPKVA MLSYSSGASG KGEDVDKVRK ATEIAKAQEP
ELKIEGPIQY DAAVDMRIGK SKLPNSEVAG QASVLIFPDL NTGNNTYKAV QRETGALAIG
PMLQGLNKPV NDLSRGCTAD DIYSTVIITA IQAQDL
//
