ID H6Q5D4_WIGGL Unreviewed; 708 AA.
AC H6Q5D4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 13-SEP-2023, entry version 50.
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:AFA41417.1};
GN ORFNames=WIGMOR_0603 {ECO:0000313|EMBL:AFA41417.1};
OS Wigglesworthia glossinidia endosymbiont of Glossina morsitans morsitans
OS (Yale colony).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=1142511 {ECO:0000313|EMBL:AFA41417.1, ECO:0000313|Proteomes:UP000009061};
RN [1] {ECO:0000313|EMBL:AFA41417.1, ECO:0000313|Proteomes:UP000009061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WGM {ECO:0000313|EMBL:AFA41417.1};
RX PubMed=22334516;
RA Rio R.V., Symula R.E., Wang J., Lohs C., Wu Y.N., Snyder A.K.,
RA Bjornson R.D., Oshima K., Biehl B.S., Perna N.T., Hattori M., Aksoy S.;
RT "Insight into the transmission biology and species-specific functional
RT capabilities of tsetse (Diptera: glossinidae) obligate symbiont
RT wigglesworthia.";
RL MBio 3:E00240-11(2012).
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; CP003315; AFA41417.1; -; Genomic_DNA.
DR RefSeq; WP_014354356.1; NC_016893.1.
DR AlphaFoldDB; H6Q5D4; -.
DR STRING; 1142511.WIGMOR_0603; -.
DR KEGG; wgl:WIGMOR_0603; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR HOGENOM; CLU_019723_2_1_6; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000009061; 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; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
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 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; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 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 388..703
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 708 AA; 80888 MW; F6AFBECFBE287CE4 CRC64;
MSRTIMLIPT EKNIGLSHVF SGIMHAISQA SILYTVFRPI DYIYEDENKF DIIKYSSSIY
NISYTSMRSQ YSLKNIIQLL CSNQKHILME NIIETFYQQQ KNSAITLIPG ISIHNKYFDF
MQLNCEIAKM LNADIILISK FNKNYFDSFV EYIEFISLPY GGTKNKRIKG VILNQINFLK
NSNIKKDLDW IRLLEVNKYK YTKKIDKNLE KLKDNNSIPI IAKIPWDSNL DFIRLYNLKK
YFNAKIINNY RKDLIIKFIA IFQNSERFLY AKYYKESLLI ILTNQINKNF YSILEKFQAI
LLVGSENNYK KIQNICNIAD NKKIILLSLE TDYLSILKKL KYLKLKYLKS NQDIFETNAY
IAKFFDNTWI SSLNTSSYIQ KIDSPQIFQY NILQLARKEL KNIILPEACD LRILKAANIC
AKKNIARCTL LGDPKNIQQI AYQNGIVLEK NIHIVNPLDI QKKYIPRIMN LRKKKEISEK
IAIKQLKNNI ILATLMLDAG VVDGLVAGAI STTADTLRPA FQFIKTTQKN SLISSIFFML
LPEKTVIYGD CAINVDPNAY QLAEIAIQSA NSAIQFGIDP KIAMISYSTG YSGTGISVEK
VRQATCIVKS KYPEFIIDGP LQYDAAMVQK ISQSKSPHSC ISGNATVLIF PDLNTGNTTY
KAVQRSANIS CIGPILQGIR KPVNDLSRGA SVEDIIYVIA VTAIQSMK
//
