ID A0A124DZA5_9MYCO Unreviewed; 700 AA.
AC A0A124DZA5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=RMCB_0859 {ECO:0000313|EMBL:GAS86763.1};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS86763.1, ECO:0000313|Proteomes:UP000069620};
RN [1] {ECO:0000313|EMBL:GAS86763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM15654 {ECO:0000313|EMBL:GAS86763.1};
RA Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT M. brisbanense, and M. novocastrense.";
RL Genome Announc. 4:e00322-16(2016).
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:GAS86763.1}.
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DR EMBL; BCSX01000011; GAS86763.1; -; Genomic_DNA.
DR RefSeq; WP_062827785.1; NZ_JACKTM010000054.1.
DR AlphaFoldDB; A0A124DZA5; -.
DR STRING; 146020.RMCB_0859; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000069620; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 211..323
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 700 AA; 73890 MW; A21164F47A07EFE4 CRC64;
MPDGNIATAI YVASPEGDTG KSTIALGILH RLAATVPRVG VFRPITRLGE DRDYILELLL
AGATAGLPYE DCVGVGYQQV HEDPDAAVAE IVDRFHRVAD RCDAVLIVGS DYTDVATPSE
LSMNARIAVN LGAPVVLAVK AADRTPEEVA HVVEVCLAEL NHQHAHAAAV VANRCDPAQL
TAVAEALKPL GTPAYVLPEE PLLVAPSVAE LQVAVDGTMI AGDPALLSRE AMGVLVAGMT
AEHVLERLTE GVAVVTPGDR SDVVLAVVSA HAAEGFPSLS CIVLNGGLDL HPSIAALVEG
LGLRLPIVAT KYGTFETASR VASARGRVTA KSQRKIDTAL ALMDKHVDVN DLLAQLSIPI
PAVTTPQMFT YQLLDRARSD RKRIVLPEGT DDRILKAAGR LLRRSVADLT ILGEESQIRS
RAAELGVNID AAVVLDPRTS ELCDQFAEQY AELRRKKGIT VEQARETIHD VSYFGTMLVH
NNMVDGMVSG AAHTTAHTVR PAFEIIRTAP GISTVSSIFL MCLADKVLAY GDCAIVPDPT
SEQLADIAIS SARTAAQFGI EPRVAMLSYS TGTSGTGADV DKVRAATELV REREPDLLVE
GPIQYDAAVE PSVAITKMPD SPVAGRATVL IFPDLNTGNN TYKAVQRSAG AIAIGPVLQG
LNKPVNDLSR GALVEDIVNT VAITAIQAQG GMTRTRGAVE
//
