ID A0A0Q6FFG9_9ACTN Unreviewed; 464 AA.
AC A0A0Q6FFG9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KQT90737.1};
GN ORFNames=ASG49_13390 {ECO:0000313|EMBL:KQT90737.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT90737.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT90737.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90737.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT90737.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT90737.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:KQT90737.1}.
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DR EMBL; LMRF01000005; KQT90737.1; -; Genomic_DNA.
DR RefSeq; WP_056542676.1; NZ_LMRF01000005.1.
DR AlphaFoldDB; A0A0Q6FFG9; -.
DR STRING; 1736379.ASG49_13390; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000051542; 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; 3.30.70.260; -; 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; 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; 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 PRINTS; PR00072; MALOXRDTASE.
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; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT DOMAIN 17..93
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 242
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 464 AA; 48473 MW; F95D8CFFF043FAD3 CRC64;
MADKKRRAAT SGSYSITVRL FTEVDPAIVG QVATAIAAEG GIVTALDVAE SRHDRIVYDV
TCSATDSEHA AEIVDHLRNL QGITVHKVSD RTFLLHIGGK IEVSSKVPLR TRDDLSMAYT
PGVGRVSLAL AENPGDVPRL TIKGNSVAVV TDGSAVLGLG NIGPGAALPV MEGKAALFKR
FANIDAWPIC LDTQDTDRIV DVVAAIAPGF GGINLEDIAA PRCFEIERRL RERLDIPVFH
DDQHGTAIVV LAALTNALRC VEKDLASIRV VVAGAGAAGT AIVTLLLAAG AADVVVCDKD
GALAEGDESL SPAMADLASR TNPRRVRGDL RTALEGADVF IGVSAPGVLQ AEWIPGMAEK
PIVFALANPD PEIDPAEAAP YAAVVASGRS DYPNQINNVL AFPGVFRGLL DARASDVTIE
MLLSAATAIA DCVSAEELNA SYIIPSVFDS KVPKAVARAI QGLD
//
