ID Q4FRZ3_PSYA2 Unreviewed; 779 AA.
AC Q4FRZ3;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Putative NADP dependent malate oxireductase {ECO:0000313|EMBL:AAZ19215.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:AAZ19215.1};
GN Name=maeB {ECO:0000313|EMBL:AAZ19215.1};
GN OrderedLocusNames=Psyc_1367 {ECO:0000313|EMBL:AAZ19215.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ19215.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ19215.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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, ECO:0000256|RuleBase:RU003427}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; CP000082; AAZ19215.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4FRZ3; -.
DR STRING; 259536.Psyc_1367; -.
DR KEGG; par:Psyc_1367; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_6; -.
DR Proteomes; UP000000546; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
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 Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 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; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 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:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAZ19215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000546}.
FT DOMAIN 38..171
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 183..419
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 96..103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 779 AA; 85406 MW; 52D381F4D322D0BB CRC64;
MAIIMNDDIT LNTDTPTPST EKEQFEQAAL HYHEFPRPGK ISVTPIKQLA NQRDLALAYS
PGVAVPCLEI QRDPSLAAKY TARSNLVGVI TNGTAVLGLG NIGPLASKPV MEGKGVLFKK
FAGIDVFDIE IAQNDPDKFI EAVASLEPTF GGINLEDIKA PECFKIEREL RKRMNIPVFH
DDQHGTSIIV AAAMLNALII TNKKIEDIKI ICSGAGAAAI SCLDIICALG VNKNNIYVSD
SRGIISTTRE NLDETKQRYA RETTATTIEE LMDDVDMFLG LSMPGTLTED MVRRMAKDPI
IFALANPTPE IMPEIAHAVR PDVIMATGRS DYPNQVNNAL CFPYIFRGAL DVGATTVNEE
MKVACVRAIA AMAHVEATPI SNIKNVESTP SFGRDYLIPG PLEPNLIIEI ASAVAKAAMD
SGVATLPIAD MKAYRQRLSE FVYNSAFVMK PIFARAKADP KRIVYCEGED RDVLLAVQVV
VDEQLAYPIL VGRPSVIENN ITKLALRLKD GENITIVNVD DDPRYNDYWK GYYEKNKRTG
VSIELARRDV RRKTSLIGAL LVENGDADGM ICGTFGHYQL HLKYVSRVIN KKEGINDFYA
MNAVLMQDRN IFIADTYIHE DPTAEQLAEM TVLATEQLRR FSITPRVALV SHSNFGTSDR
ASAVKMRKVH QLLTEMNVDF EFDGEMQGDA ALDEHIRAND LPSSNLKGSA NLLILPTLDA
SNIAFNLLKT ATGSASIGPI LLGASKPVHI LTPSATARRV VNMTALAVTE AQDLENKQQ
//
