ID L7VKG0_9FLAO Unreviewed; 692 AA.
AC L7VKG0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 13-SEP-2023, entry version 47.
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 Name=pta {ECO:0000313|EMBL:AGC66981.1};
GN ORFNames=ASNER_227 {ECO:0000313|EMBL:AGC66981.1};
OS Candidatus Uzinura diaspidicola str. ASNER.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Candidatus Uzinura.
OX NCBI_TaxID=1133592 {ECO:0000313|EMBL:AGC66981.1, ECO:0000313|Proteomes:UP000011174};
RN [1] {ECO:0000313|EMBL:AGC66981.1, ECO:0000313|Proteomes:UP000011174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASNER {ECO:0000313|EMBL:AGC66981.1,
RC ECO:0000313|Proteomes:UP000011174};
RX PubMed=23279075; DOI=10.1111/1462-2920.12058;
RA Sabree Z.L., Huang C.Y., Okusu A., Moran N.A., Normark B.B.;
RT "The nutrient supplying capabilities of Uzinura, an endosymbiont of
RT armoured scale insects.";
RL Environ. Microbiol. 15:1988-1999(2013).
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; CP003263; AGC66981.1; -; Genomic_DNA.
DR AlphaFoldDB; L7VKG0; -.
DR STRING; 1133592.ASNER_227; -.
DR KEGG; udi:ASNER_227; -.
DR PATRIC; fig|1133592.3.peg.210; -.
DR HOGENOM; CLU_019723_3_0_10; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000011174; Chromosome.
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:UP000011174};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 207..321
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 368..685
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 692 AA; 78358 MW; 631ACE3CEA3FD95B CRC64;
MIKNSVFIFS TDLYSGKSLA TFGIMQMIMK KKHCLAIFRP IIEESCYSVK DDHIYAVISH
FQLKIFYEET FCFSRKEAIF LYKYGGNHRI YDHIFKKHKE LEGSFDFVLV EGQDYYNDNR
DIELNTEVAK HLQLPIILVM NGANKNIKTV YDHIRRQHVN FIILVINKTL IPFQLLQSYL
TRYLPPEVVV FTVPPDDILD KPTIIEIQKE FDAKLIIGSK YDLNKISITY IISSFLYCNQ
SFPLSILNED LLIITQGDRI DLILATLIAN ISSKYGHISA LILTGSILPE ETFLNIMKSV
PNFIPILAGY CDTLETSQRV ASIRTHCCSQ NMVKLQHSIN LFEEYVENPL LFEKITLKKY
KYITPQIFHY NIVKQSKIAQ KHIVLPEGND ERILLAASFF SKEGLGKITI LGNPKKIMAK
VNSLGISWEE ERITILDPVS SNFYEDFYST LYHLRKEKGL KLTEAKNLML DISYFGTMMV
YKGLADGMVS GAENTTASTI RPALQFIRTR TDINTVSSIF FMLLKDRVLV YGDCAIVPDP
TAEQLADITI VSAKTAEDFG FEPKVALLSY SSGHSGSGKQ VEKVRIATEI VKNRAPKLLV
EGPIQYDAAV DPKVGKKKLP NSHVAGSANV FIFPELNTGN NTYKAVQRET KSLAIGPVIQ
GLNRPINDLS RGASVEDIYH TLLITSIQSI RN
//
