(data stored in SCRATCH zone)

SWISSPROT: A4AV55_MARSH

ID   A4AV55_MARSH            Unreviewed;       698 AA.
AC   A4AV55;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Phosphate acetyltransferase {ECO:0000256|PIRNR:PIRNR006107};
DE            EC=2.3.1.8 {ECO:0000256|PIRNR:PIRNR006107};
DE   AltName: Full=Phosphotransacetylase {ECO:0000256|PIRNR:PIRNR006107};
GN   OrderedLocusNames=FB2170_00385 {ECO:0000313|EMBL:EAR00077.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00077.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00077.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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
CC       biosynthesis; acetyl-CoA from acetate: step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR006107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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
CC       substrate-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|PIRNR:PIRNR006107}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ
CC       family. {ECO:0000256|PIRNR:PIRNR006107}.
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DR   EMBL; CP002157; EAR00077.1; -; Genomic_DNA.
DR   RefSeq; WP_013304772.1; NC_014472.1.
DR   STRING; 313603.FB2170_00385; -.
DR   EnsemblBacteria; EAR00077; EAR00077; FB2170_00385.
DR   KEGG; fbc:FB2170_00385; -.
DR   eggNOG; ENOG4108H2Z; Bacteria.
DR   eggNOG; COG0280; LUCA.
DR   eggNOG; COG0857; LUCA.
DR   HOGENOM; HOG000053797; -.
DR   KO; K13788; -.
DR   OMA; TPLMFEY; -.
DR   OrthoDB; 1301815at2; -.
DR   BioCyc; MSP313603:G1GNS-345-MONOMER; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001602; 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; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 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   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AV55.
DR   SWISS-2DPAGE; A4AV55.
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR006107,
KW   ECO:0000256|SAAS:SAAS00923789};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006107,
KW   ECO:0000256|SAAS:SAAS00923780, ECO:0000313|EMBL:EAR00077.1}.
FT   DOMAIN      215    326       DRTGG. {ECO:0000259|Pfam:PF07085}.
FT   DOMAIN      372    691       PTA_PTB. {ECO:0000259|Pfam:PF01515}.
SQ   SEQUENCE   698 AA;  76776 MW;  ABBDB8CA1D559BD5 CRC64;
     MSKAIYIATT EPNSGKSIIS LGLMQMLLGK AAKVGYFRPI IDDYTNGTKD NHIKTIISYF
     NLPIAYEDAF AFTRSEVIQM NNQNKEDEVL DKIIEKYKSI EDQFDFVLVE GTDFSGEGAI
     IEWDINVLMA KNLGIPTLIL TSGVGKTLDE LVNNVYLAYD SFKDHGVEVL MVVANKVQEK
     NLELVNESLQ KVIPEEVLVG SIPMNPVLGN PTIKEIVDVL EGKVLFGEKY LNNQAGHFGV
     GAMQLRNYLT HLKKDGLVIT PGDRADIILG ALQANLSANY PTVSGMILTG GIIPEEPIAK
     LIEGLSDVVP IISVEEGTFS ITNRIGAIRP KIYAENTHKI MTSIQDFSKY IPEEVLAKRL
     ITSKSKGITP RMFQYNLLKR AKADKKRIVL AEGLDERVLK ATKQLLDANA VEITLLGDPI
     QIADKISLMD LDLDLNSIEI ENPTESKYFD EFSETLYELR KHKNVNLAMA RDLMEDVSYF
     ATMMVHKGYA DGMVSGAIHT TKHTILPALH FIKTRPDVSV VSSVFFMCLE DRVTLYGDCA
     INPNPDAEQL SEIAISSAET SQAFGIDPKI AMLSYSSGSS GVGEDVERVR NATKLVKEKR
     PDLKVEGPIQ YDAAVDINVG KTKMPGSQVA GEASVFIFPD LNTGNNTYKA VQRETGTIAI
     GPILQGLNKP VNDLSRGCNV DDIFNAVIIT AIQAQDLE
//

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