ID I2AK13_9MYCO Unreviewed; 716 AA.
AC I2AK13;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=W7S_23440 {ECO:0000313|EMBL:AFJ37637.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ37637.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ37637.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ37637.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(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 -!- 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; CP003491; AFJ37637.1; -; Genomic_DNA.
DR RefSeq; WP_014712472.1; NC_017904.1.
DR AlphaFoldDB; I2AK13; -.
DR KEGG; mmm:W7S_23440; -.
DR PATRIC; fig|1168287.3.peg.4767; -.
DR HOGENOM; CLU_019723_3_1_11; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000002868; 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; 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 234..345
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 392..709
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
FT REGION 44..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 75596 MW; E58B2E3949924D13 CRC64;
MVSGAATAIY IAAPEPETGK STIALGLLHR LTATVAKVGV FRPITRSDGG DRQRGEAGRS
GSPQDRGDRD YILELLLSRT TAGLSYEQCV GVTYQQLHAD GDAAIAAIVD AYHAVAEQCD
VVVIVGSDYS ELGQAIRPAE LSTNARIAVN LGAPLLLTVS GKGRTAGEVA DVVKVCLAEL
DAQHAHTAAV VANRCEPAEL DAIRKKLDEA LRPSSLRSYV LPDEPLLSAP TVAELQSAVR
GTPVSGEESL REREVTGVMV AGMTADHVLE RLRDGMAVIT PGDRSDVVLA VASAHAAEGF
PSLSCIVLNG GFELHPSIAA LVAGLRLRLP IVATALGTYD TASAAASARG SVTAASQRKI
DTAVELMDGH VDITDLLAQL AIPIPTVTTP QMFIHQLTLQ ARSDRRHIVL PEGDDDRILR
SAGRVLQRRV ADLTILGDEA QIRQRAGELG VDLADVTVID PRASRLRDEF ADQYAQLRKA
KGVTVEQARE IMRDTTYFGT MMVHNGMVDG MVSGAAHTTA HTVRPAFEII KTVPDVSTVS
SIFLMCLPDR VLAYGDCAII PNPTPEQLAD IAISSARTAA QFGIEPRVAM LSYSTGDSGS
GADVDKVRTA TQLVRERNPD LPVEGPIQYD AAIEPSVAAT KLRDSPVAGR ATVLIFPDLN
TGNNTYKAVQ RSAGALAIGP VLQGLRKPVN DLSRGALVED IVNTVAITAI QAQGGP
//
