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Database: UniProt
Entry: A0A0L6CMQ6_9MICO
LinkDB: A0A0L6CMQ6_9MICO
Original site: A0A0L6CMQ6_9MICO 
ID   A0A0L6CMQ6_9MICO        Unreviewed;       699 AA.
AC   A0A0L6CMQ6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=VV01_21225 {ECO:0000313|EMBL:KNX39076.1};
OS   Luteipulveratus halotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Luteipulveratus.
OX   NCBI_TaxID=1631356 {ECO:0000313|EMBL:KNX39076.1, ECO:0000313|Proteomes:UP000037397};
RN   [1] {ECO:0000313|Proteomes:UP000037397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C296001 {ECO:0000313|Proteomes:UP000037397};
RA   Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA   Yeo T.;
RT   "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT   (Dermacoccaceae) from Sarawak, Malaysia.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KNX39076.1}.
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DR   EMBL; LAIR01000002; KNX39076.1; -; Genomic_DNA.
DR   RefSeq; WP_050671631.1; NZ_LAIR01000002.1.
DR   AlphaFoldDB; A0A0L6CMQ6; -.
DR   STRING; 1631356.VV01_21225; -.
DR   PATRIC; fig|1631356.3.peg.4272; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000037397; 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   CDD; cd03109; DTBS; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000037397};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT   DOMAIN          211..322
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   699 AA;  73625 MW;  2A5D2CBD53234A0A CRC64;
     MSRSVYITST EGETGKSTIA LGLLDLLSRE TGRVGVFRAV TASDQRRDPV VELLLDHAGV
     DQSYDESIGV TYQRLHSDEP GALADIVDRF HRLSATRDVV VVLGSDFTDV ASGAEGALNA
     RIAANLGSPV VLVVQGKDRT PAELVIATEA ACEQLRDEHA LPVALVANRV ADDLVDEVRT
     RLTDLPAAGG APLVGVLPEV PLLVAPTVRS LMEACDGELL RGNEAWLDRE ARGFVIAAMS
     MPNVLTRLVE DVTVIAPGDR YDVLPGLMFA HQSGTFPGLS SVVLTGGYVP PDTILQLIDG
     SPSDLPIILT QLGTFDTTTR LAGTKGALST GSVAKRQTAM RAFAESVDGP ALLAAIDVGE
     ALAVTPLMFT HRLLERARSE RKRIVLPEGD DPRILQAADS LLRQGVADLV LLGDETALRA
     KASSAGLDIT GATVLSPTDE EHVERFAKVY TELRAHKGMT VEKARKVVSD VSYFGTLMVH
     LGEADGMVSG AAHTTAHTIK PSFEIIKTVP GTSVVSSVFL MCLADRVLVY GDCAVNPDPT
     AAELADIAIS SAATAERFGV EPRIAMLSYS TGTSGAGADV DKVREATELV RSRRPDLLVE
     GPIQYDAAVD PGVARSKMPD SEVAGRATVL IFPDLNTGNN TYKAVQRSAG AVAVGPVLQG
     LNRPVNDLSR GALVEDIIST VAITAIQSAS TVEAQGDSK
//
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