ID   A0A2S8SWR1_9BACT        Unreviewed;       504 AA.
AC   A0A2S8SWR1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:PQV65233.1};
GN   ORFNames=B1R32_102242 {ECO:0000313|EMBL:PQV65233.1};
OS   Abditibacterium utsteinense.
OC   Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC   Abditibacteriaceae; Abditibacterium.
OX   NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV65233.1, ECO:0000313|Proteomes:UP000237684};
RN   [1] {ECO:0000313|EMBL:PQV65233.1, ECO:0000313|Proteomes:UP000237684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV65233.1,
RC   ECO:0000313|Proteomes:UP000237684};
RX   PubMed=29475572;
RA   Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT   "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT   candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL   Syst. Appl. Microbiol. 0:0-0(2018).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:PQV65233.1}.
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DR   EMBL; NIGF01000002; PQV65233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8SWR1; -.
DR   InParanoid; A0A2S8SWR1; -.
DR   Proteomes; UP000237684; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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; 3.30.70.260; -; 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; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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; 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; PF13291; ACT_4; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237684}.
FT   DOMAIN          45..119
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   504 AA;  53789 MW;  3C9140017180BB79 CRC64;
     MVLWRDSTTL KVGAFKVVES KRIASLQPLK LSAMASRPSP SYSLTLRVEY SNRLGMLGRI
     TSLIGERGGD IGAIDIVQST KGAMTRDITF SAANVDHGKQ IIEAVRDLGE VDIVQVSDRT
     FLLHLGGKLE ITPKVPVKTR DDISMIYTPG VARIVEKIVE NADDAFNLTI KKNTVAVITD
     GSEVLGMGAA GPQAALPVME AKAILFKEFA GVDAFPLPLD VETDEEFVAA VRAIAPAFGA
     IHIEDIAAPR CFRLEKMLTE ALDIPVFHND QHGTAIVALA GLINALKIIG KSAQSLRVVI
     NGAEAAGVAT AKLLIAFGVR DIILCDERGI LSADQDDETL LEMAQNTNPR KVSGGIVEAL
     VGADALMGFG HRTVLEPSAI EAMNVNPIVF AMANPNPEIE PSRIAEIARV IATGKSDFPN
     QINNMLCFPG FFRGLLDARA TKVNDEMKLA AAHAIAGVIG PEELHEDYLI PSVFNRRVAN
     AVARAVAKAA QDSGAARKAL RPSL
//