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Database: UniProt
Entry: C5ZX35_9HELI
LinkDB: C5ZX35_9HELI
Original site: C5ZX35_9HELI 
ID   C5ZX35_9HELI            Unreviewed;       315 AA.
AC   C5ZX35;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EES89703.1};
GN   Name=citH {ECO:0000313|EMBL:EES89703.1};
GN   ORFNames=HCAN_0989 {ECO:0000313|EMBL:EES89703.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89703.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES89703.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(2009).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CM000776; EES89703.1; -; Genomic_DNA.
DR   RefSeq; WP_006655691.1; NZ_DS990368.1.
DR   AlphaFoldDB; C5ZX35; -.
DR   STRING; 537970.HCAN_0989; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_7; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000007032; Chromosome.
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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01339; LDH-like_MDH; 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; IPR001557; L-lactate/malate_DH.
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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          6..144
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          149..302
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         120..122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   315 AA;  34069 MW;  D90937C31F556DB9 CRC64;
     MERVKRVGII GAGNVGSTLA YILSATTPYQ IVLRDKDKDR ARGMLLDMFQ ASCVGEKFAK
     LDVIASPKDL GGCDVIVVAA GSPRLPGMSR NDLLFANAKV IGEIAKDIKE NSPEAIVILV
     TNPLDAMVYT MLRETGFNPR QILGMAGILD SARMASFIYE KLQCAPGQIV APVMGGHGDD
     MVPLPRFCMV NGVPLNELLE ESQIEEVVQR TRNAGAEIVS CLKKGSAYFA PARATAEMVC
     AIMSDSHKIL PCSVLLQGEY GYHDVVGGVP VELGIHGIER VVELKLLPEE KQQFDKSIQS
     VQGLIDALKT DYFNS
//
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