ID A0A0N1HDN1_9EURO Unreviewed; 1255 AA.
AC A0A0N1HDN1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN ORFNames=AB675_9875 {ECO:0000313|EMBL:KPI42617.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI42617.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI42617.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI42617.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family.
CC {ECO:0000256|ARBA:ARBA00005234}.
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:KPI42617.1}.
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DR EMBL; LFJN01000007; KPI42617.1; -; Genomic_DNA.
DR RefSeq; XP_018002580.1; XM_018150448.1.
DR AlphaFoldDB; A0A0N1HDN1; -.
DR STRING; 1664694.A0A0N1HDN1; -.
DR GeneID; 28742328; -.
DR OrthoDB; 5059897at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019783; F:ubiquitin-like protein peptidase activity; IEA:UniProt.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 711..889
FT /note="Ubiquitin-like protease family profile"
FT /evidence="ECO:0000259|PROSITE:PS50600"
FT REGION 368..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..195
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 563..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 136624 MW; F0BDA32E3EF7BD63 CRC64;
MSEVDAMDWQ PMLTPPHPHP IAPYYYTGYM PGGWPERTLD RPNTQYRRPA PDSQWIERDL
KRVCRGIELA GDAACQGARA AGKGAGRLAV AGARRAGQET LRGTVAVGRV GFAVAKKAAV
TTSNSTIAII RRCQRNSPRD LQKRAQAEAK RAAMKRKLAD ILAREQKRKS LACHAAQEEQ
RKRAYEVAQE AAQEAKAIDT PINVSPKTGI MLAHLAQAEA QAEARNAAAT EAANAELLQR
FLQRKIFQGR GTAFARRAIK LQPRRPQGIT KYLPSPRRVR NPYSTMLSYD HNEKGTQTDP
VAQKEENLAE HVAYWQNLER TGASEVDVHA TYIHSSDRAT QMNRPLFPRT SVDLDALAIE
ALEQSTEVQT ATKTTQPTYS KAAPTGTQNK TLKTPKTAAL QRVPQTGYSN ISSTVEHTPV
QPIAVTPARP KRVEALAATP AKPQTPFSDI SSTVEMTPPQ VQATHAMPQT PLSDISSTFR
ETPPKPQTPL SNILSTVTKT FARAKATEPK DRTPYSDISS NVAPTPVRTE PIKAKHQTPY
SDISSNVAPT PIPAYHTVQS VADAVGSPSS STKAPGKSPL PRTSHVGITK SPPGAWIDEE
TTMEQDQKSK EATITLTFRT PARRAVSNKA LRGLSDDEKK EEIKERVRTP PEHETPPKSS
VHGRKRDRTK QEIKERQEEA QKKKNQYTIT PLSDEWDDKV EEYIQNGLPE AELTAKDLGR
CAPPRDASAN HDNWLNDEVI NKYLKMVTEY GNNLAGRPRD KTPAFHAFTS FFYSKMADPK
QGVKTILRWV NKARIGGKRM LETEMVFVPI NSGSHWTLAV VSGVNRTISY YDSLGSKRSS
YMEVLLGWLE VELGDAFVRS EWKLQVEESG RQANMDDCGV FTVTNARSLV LGVKPHEFAG
EELAQFSSIT AANMVKVGIL GASGGIGQPL SLLCKISPLI DEITLWDVVN TPGVAADLGH
ISSKAKLTGH VAAKGDFAMK QDESNAAQKE ALSGLDIAII PAGVPRKPGM TRDDLFKINA
GIVKGLVEAL AKYSPKAYVL VISNPVNSTV PIAAEVLTAA GVFDAKKLFG VTTLDVVRAE
TFVAEVTGSK EVPDKTTIPV VGGHSGNTIV PLFSQAKPAV NIPEDKLDAL VHRVQFGGDE
VVKAKDGAGS ATLSMAYAGF RFAEAVLKAK KGEKGIVEPA FVYLPGVPGG EEIQKATGVD
YFSAPVEFGP NGVEKVINVL SNVNDYEKKL LDEAVKGLKT NIETGVDFVK NPPQK
//
