ID A0A0Q9S5D6_9MICO Unreviewed; 484 AA.
AC A0A0Q9S5D6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KRF23101.1};
GN ORFNames=ASG91_16655 {ECO:0000313|EMBL:KRF23101.1};
OS Phycicoccus sp. Soil802.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF23101.1, ECO:0000313|Proteomes:UP000050906};
RN [1] {ECO:0000313|EMBL:KRF23101.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF23101.1,
RC ECO:0000313|Proteomes:UP000050906};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF23101.1, ECO:0000313|Proteomes:UP000050906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF23101.1,
RC ECO:0000313|Proteomes:UP000050906};
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|ARBA:ARBA00001946};
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:KRF23101.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMSS01000006; KRF23101.1; -; Genomic_DNA.
DR RefSeq; WP_056923839.1; NZ_LMSS01000006.1.
DR AlphaFoldDB; A0A0Q9S5D6; -.
DR Proteomes; UP000050906; 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; 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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU003427}.
FT DOMAIN 93..226
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 238..464
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 484 AA; 50652 MW; D41698B007CD87A8 CRC64;
MTAAPSVSNS ITVRLTLPAR ATAVSELTGV IEKGGGLVTG LDVTASGADR LRVDVTAAAR
DTDHADELVA AMRGVHGVEI GKVSDRTFLA HLGGKLKIES KVPIRNRDDL SLIYTPGVAR
VCMAIAENPE DARRLTIKRN TVAVVTDGSA VLGLGNIGPL AALPVMEGKA ALFKRFADID
AFPICLDTQD TEEIIRTVKA LSPVFAGINL EDISAPRCFE IEARLRDELD IPVFHDDQHG
TAIVTLAALR NALRVVGKEL SECRVVMSGA GAAGTAILKL LLKAGATDVV VADQFGVLHR
DRDDIASGEH PALAWSAEHT NHRGVTGTLK QAIAGADVFV GVSAPGILTG DDIATMNDGA
IVFAMANPEP EVDPIAAAQH AAVVATGRSD FANQINNVLV FPGVFRGLLD AASTSIDEDV
MLAAAKALSE VVHPEELNAA YIIPSVFHPD VSKVVAAAVK AAVLGTTPEQ VPTRRMAEEP
EFIG
//
