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Database: UniProt
Entry: U1JXV5_9GAMM
LinkDB: U1JXV5_9GAMM
Original site: U1JXV5_9GAMM 
ID   U1JXV5_9GAMM            Unreviewed;       413 AA.
AC   U1JXV5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Phosphotransacetylase {ECO:0000313|EMBL:ERG25494.1};
GN   ORFNames=PMAN_13869 {ECO:0000313|EMBL:ERG25494.1};
OS   Pseudoalteromonas marina DSM 17587.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG25494.1, ECO:0000313|Proteomes:UP000016528};
RN   [1] {ECO:0000313|EMBL:ERG25494.1, ECO:0000313|Proteomes:UP000016528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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:ERG25494.1}.
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DR   EMBL; AHCB02000038; ERG25494.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1JXV5; -.
DR   Proteomes; UP000016528; 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   CDD; cd05311; NAD_bind_2_malic_enz; 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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   PIRSF; PIRSF000106; ME; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          17..150
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          162..398
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        38
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   413 AA;  44581 MW;  270DD6037FA31FFB CRC64;
     MSDFREQALH YHSHPVPGKI SIELTKPAET VKDLALAYSP GVAEPVREIA ADPANAYKYT
     GKGNMVAVIT NGTAILGLGN LGPLASKPVM EGKALLFKRF AGLDSIDIEV KHRTTEDFIN
     TVANIADTFG GINLEDIKAP ECFEIEKALI ERCSIPIFHD DQHGTAIVTA AGMLNALEVQ
     GKSIENATIV CLGAGAAAVA CMELLIKCGA LREHIYMLDR KGVIHTRRDD LNEYKKLFAN
     NTDKRTLQDV IEDADVFVGV SGPNLLAADD LKLMAEKPVV FACSNPDPEI DPALAHSARN
     DLIMATGRSD YPNQVNNVLC FPFIFRGALD VRASAINDEM KIAAVEAIRS IAKEPVPAEV
     LTAAGVDKLE FGNKYIIPKP MDPRLLPRIA KAVAIAAVES GVAQIDLPEN YME
//
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