ID A0A1J0KT38_9GAMM Unreviewed; 602 AA.
AC A0A1J0KT38;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Malic enzyme, NAD binding domain protein {ECO:0000313|EMBL:APC96814.1};
GN ORFNames=KX01_17 {ECO:0000313|EMBL:APC96814.1};
OS Francisella frigiditurris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=1542390 {ECO:0000313|EMBL:APC96814.1, ECO:0000313|Proteomes:UP000182521};
RN [1] {ECO:0000313|Proteomes:UP000182521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA97-1460 {ECO:0000313|Proteomes:UP000182521};
RA Kuske C.R., Challacombe J.F., Daligault H.E., Davenport K.W., Johnson S.L.,
RA Siddaramappa S., Petersen J.M.;
RL Submitted (OCT-2014) 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}.
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DR EMBL; CP009654; APC96814.1; -; Genomic_DNA.
DR RefSeq; WP_071663060.1; NZ_CP009654.1.
DR AlphaFoldDB; A0A1J0KT38; -.
DR STRING; 1542390.KX01_17; -.
DR KEGG; frc:KX01_17; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000182521; Chromosome.
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:0008152; P:metabolic process; IEA:UniProt.
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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 89..269
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 279..560
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 254
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 255
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 602 AA; 67199 MW; 3753C7AF1F124BD8 CRC64;
MEKKRIRKLR NKTGRVFAIE TNLSGRQLLN NRVLNKDVAF SQEERIAFDL VGLLPEKVES
LEEQAARVRK QLDLKPSNLE KFVFLNRLHD LNTTLFYHFL RSNLEEVMPI IYTPTVGEAV
QKYSSSFRKQ SGLFLSINHK KDIGRILERY DYNSIDLILV TDGEAVLGIG DQGIGGMNIS
IGKLMVYVAA SGIDPARVLP VQLDMGTNND ELLSAPGYLG MRLPRVSGET YDEFIEEFVK
ELKTRFPNVF LHWEDIGRDN AQRILDKYKD KLCTFNDDIE GTGIVATANV IAGIKTANRI
RINAGELTTE EAIADIENTR IVIYGAGSAG CGIANQLADV ISDLTGLPFE KAANCIYLID
RYGLVTDKIK PKRITEGQRP FVKSSKLLEK WKVKDPNYIT LEETVRHTEA DVLIGTSGRP
GAFTEEVIRD MAKFNNYPII MPLSNPTSLC EAIPEDIIKW TEGKALIAAG SPFPDVEFNG
RTYRISQGNN AFIFPGLGLG SVAVHAKKLT KGMIRAACYR LSELSPMVIN EDITQPLLAK
ITDLVEVSFE ITKAVAKQAI EEGVHGVDID LEDITPEEFD AEVERLINMS SWTPTYAPYM
PI
//
