ID   A5CPD4_CLAM3            Unreviewed;       705 AA.
AC   A5CPD4;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-OCT-2025, entry version 94.
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=ptaA {ECO:0000313|EMBL:CAN00932.1};
GN   OrderedLocusNames=CMM_0895 {ECO:0000313|EMBL:CAN00932.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN00932.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN00932.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN00932.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA   Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
CC   -!- FUNCTION: Involved in acetate metabolism.
CC       {ECO:0000256|ARBA:ARBA00049955, 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|ARBA:ARBA00000705,
CC         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; AM711867; CAN00932.1; -; Genomic_DNA.
DR   RefSeq; WP_012037580.1; NC_009480.1.
DR   AlphaFoldDB; A5CPD4; -.
DR   GeneID; 92946856; -.
DR   KEGG; cmi:CMM_0895; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_1_11; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001564; 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   CDD; cd03109; DTBS; 1.
DR   FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 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; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR   InterPro; IPR002505; PTA_PTB.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   NCBIfam; NF004167; PRK05632.1; 1.
DR   NCBIfam; NF007233; PRK09653.1; 1.
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:UP000001564};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          221..334
FT                   /note="DRTGG"
FT                   /evidence="ECO:0000259|Pfam:PF07085"
FT   DOMAIN          380..696
FT                   /note="Phosphate acetyl/butaryl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01515"
SQ   SEQUENCE   705 AA;  74363 MW;  038050B5F54A96A9 CRC64;
     MARSIYITSA EGHSGKSTVA LGVLDTLTHQ IQRVGVFRPI ARSIEEPDYV LQALLAHDGV
     DLDYDECVGV TYDDVHADPE AALSRIVERY KAVEAKCDAV VIVGSDYTDV GSPTELSFNA
     RIAANLGAPV LLVLTGRRAD ETGGRSPDEM RQIADLAVPE LVTAHAALLG VVVNRADPEQ
     LDAITAAIPA AVPASLQARA PHVPVWAIPE DAFLVAPTVA ELLDAVDGTL VKGDQALLSR
     EALGVVVSAM SMENVLARLT EGAIVVIPGD RSEVLLGVLT AHASETFPTV AGIVLNGGFA
     LSPTIETLIA GLDQTLPIIS TELGTYETAK RITQTRGRLS PESTRKMDTA LAAFEQHVDT
     SRLLELLDVS RSDVVTPLMF EYGLIERART AGKRIVLPEG TDDRVLRAAG TILSRGIADV
     TILGEEIEVR SRAIGLGIDI GRATVLSPFD AVLRERFAEE YVRLRAHKGM VLDIARETVT
     DVSYFGTLMV QLGLADGMVS GAAHTTAHTI RPGFEIIKTT EGVSVVSSVF LMALADRVLV
     YGDCAVNPDP TADQLADIAI SSAETAAQFG IEPRIAMLSY STGESGAGAD VEKVRQATAR
     VRELRPDLAV EGPIQYDAAA DAAVAATKMP GSAVAGRATV FIFPDLNTGN NTYKAVQRSA
     GAVAIGPVLQ GLRKPINDLS RGALVQDIVN TVAITAIQAE GIEAS
//