ID A3V2D9_9RHOB Unreviewed; 751 AA.
AC A3V2D9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Phosphate acetyltransferase {ECO:0000313|EMBL:EAQ07520.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:EAQ07520.1};
GN ORFNames=SKA53_11823 {ECO:0000313|EMBL:EAQ07520.1};
OS Yoonia vestfoldensis SKA53.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ07520.1, ECO:0000313|Proteomes:UP000004507};
RN [1] {ECO:0000313|EMBL:EAQ07520.1, ECO:0000313|Proteomes:UP000004507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ07520.1,
RC ECO:0000313|Proteomes:UP000004507};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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:EAQ07520.1}.
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DR EMBL; AAMS01000002; EAQ07520.1; -; Genomic_DNA.
DR RefSeq; WP_007206306.1; NZ_CH672414.1.
DR AlphaFoldDB; A3V2D9; -.
DR STRING; 314232.SKA53_11823; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000004507; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EAQ07520.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004507};
KW Transferase {ECO:0000313|EMBL:EAQ07520.1}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 751 AA; 80955 MW; 02617C8E5D5F670F CRC64;
MAKNKLTRED ALQFHMQPTP GKWEIQATVP MTTQRDLSLA YSPGVAIPCE EIFANPATAY
DYTNKGNLVA VISNGTAVLG LGNLGALASK PVMEGKSVLF KRFADVNSID IELDTEDPDA
FCNAVRLMGP TFGGINLEDI KAPECFIIEQ RLKEEMDIPV FHDDQHGTAV ICAAGLLNAL
YLSGKKIEDV KIVLNGAGAA GIACLELLKS MGARHDNCIM ADTKGVIYQG RTEGMNQWKS
AHAVVTDARS LADAMKDADV FLGVSAKGAV TQDMVASMAP NPVIFAMANP DPEITPEEAH
AVRPDAIVAT GRSDYPNQVN NVLGFPYLFR GALDIHARAI NDEMKIACAE ALAALAREDV
PDEVAMAYGK KLSFGRDYII PTPFDPRLIH RIPTAVARAG MKTGVARRPI VDMDAYELSL
KSRMDPTASI LRSLNARARA AQSTVVFAEG DDPRVLRAAV LYQRAGMGKA LVVGRSDDVR
AKLTAEGLAE AVDEIEVVNA ANTIHLETYK AFLYKRLQRN GFDAQDIHRL AARDRHVFAA
LMLAHGHADG MVTGATRKSA HVLELINHVF DAQPHDGAVG VTAVLHKGRI VLITDTLVHE
WPDENDLADI AERGASVARD LGLEPRVAFL SFSTFGSPVS ERAEKMRKAP VVLDNRRVDF
EYEGEMTVDV ALNPRAQENY PFSRLTGPAN VLVVPARHSA SISVKLMQEM AGATVIGPIL
SGVGKPVQIC STVSTVNDIL NMAVIAACGI D
//
