ID A0A329QHL5_9ACTN Unreviewed; 718 AA.
AC A0A329QHL5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DPM12_15395 {ECO:0000313|EMBL:RAW11855.1};
OS Phytoactinopolyspora halophila.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Phytoactinopolyspora.
OX NCBI_TaxID=1981511 {ECO:0000313|EMBL:RAW11855.1, ECO:0000313|Proteomes:UP000250462};
RN [1] {ECO:0000313|EMBL:RAW11855.1, ECO:0000313|Proteomes:UP000250462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 96934 {ECO:0000313|EMBL:RAW11855.1,
RC ECO:0000313|Proteomes:UP000250462};
RA Tang S.-K.;
RT "Phytoactinopolyspora halophila sp. nov., a novel halophilic actinomycete
RT isolated from a saline soil in China.";
RL Submitted (JUN-2018) 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:RAW11855.1}.
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DR EMBL; QMIG01000018; RAW11855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329QHL5; -.
DR OrthoDB; 9808984at2; -.
DR UniPathway; UPA00340; UER00459.
DR Proteomes; UP000250462; 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 Reference proteome {ECO:0000313|Proteomes:UP000250462};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006107}.
FT DOMAIN 231..337
FT /note="DRTGG"
FT /evidence="ECO:0000259|Pfam:PF07085"
FT DOMAIN 383..700
FT /note="Phosphate acetyl/butaryl transferase"
FT /evidence="ECO:0000259|Pfam:PF01515"
SQ SEQUENCE 718 AA; 76333 MW; DE5DACB5412FD92B CRC64;
MARNVYLASV TGETGKSTVA LGILTALTRR IGRVGVFRPI VRSSAGTARP AEPAGQDGSP
DSTAVTAPSD YVLDLLLAHD GVDLPYEMCA GVTYKDVHAD RDAALGTIVD RYHRMAEHCD
AVLVVGSDYT DVDNPTEFSF NARIAANLGT PLLLVLNGRG RSPEELRAMA DSAATEVAAN
SGQLLGIVAN RVEPDAVDTI RTALGAMSPA FALPEEQLLS APTVADLVDH GGTLYRGDPA
HLGREVHDFV IAGMTLPHVL DRLTEGSVVI TPSDRSDVLI GVLMAHSART FPALTGVVLN
GGFDLPPQIT NLIDGLDVNL PIITMPGDTF TTATALAGVR GRLTRDATRK VETALTLFDE
HVDEEALLDL VDVAESSAVT PLMFEHRLVD RARQHRRHIV LPEGVDERIL RAADSVLRRG
IADLTVLGDP DRVREAATHA GADVSAATII DPHRSAWRER FAEEYARRRA HKGATVEAAH
DQIVDVSYFG TMMVLFGYAD GMVSGAIHTT ADTIRPAFEV IKTGSDVSTV SSVFFMCLRD
RVLVYGDCAV NPDPRAEQLA DIAISSAQTA EEFGVPPRVA MLSYSTGESG TGADVDKVRT
ATTLARSRRP DLSIEGPIQY DAAVDAGVAR TKLPDSEVAG RATVFVFPDL NTGNNTYKAV
QRSADAVAIG PVLQGLRKPV NDLSRGAQVR DIVNTIAITA IQAQAVGEDA AAAKDATR
//
