ID C4FAI7_9ACTN Unreviewed; 357 AA.
AC C4FAI7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative L-lactate dehydrogenase {ECO:0000313|EMBL:EEP44121.1};
GN ORFNames=COLINT_03079 {ECO:0000313|EMBL:EEP44121.1};
OS Collinsella intestinalis DSM 13280.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=521003 {ECO:0000313|EMBL:EEP44121.1, ECO:0000313|Proteomes:UP000003295};
RN [1] {ECO:0000313|EMBL:EEP44121.1, ECO:0000313|Proteomes:UP000003295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13280 {ECO:0000313|EMBL:EEP44121.1,
RC ECO:0000313|Proteomes:UP000003295};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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:EEP44121.1}.
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DR EMBL; ABXH02000019; EEP44121.1; -; Genomic_DNA.
DR RefSeq; WP_006723298.1; NZ_GG692710.1.
DR AlphaFoldDB; C4FAI7; -.
DR STRING; 521003.COLINT_03079; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_2_11; -.
DR Proteomes; UP000003295; Unassembled WGS sequence.
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 CDD; cd05291; HicDH_like; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF34; 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|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 38..178
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 183..345
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 43..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 154..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 357 AA; 39014 MW; 2410D83F970752AC CRC64;
MCQNEVASLY LGTVLGANYN YPYANFGRKD SDMYQTRKIG VIGQGHVGAH VANSLLMQGI
ADELYLCDIN ETKVTSEVQD LRDSLSFVPY NTKIVNCGDR YEELSCCDIV VNAAGKVALA
ATNRDGELFY TTDAARTFAN RVVDAGFDGI FVSISNPCDV VCTELWHLTG YDPKKIIGSG
CGLDSARLRT EISKQIGISP KSIDAYMIGE HGFSQIGAFK AATIAGKKLS ELEAENPEKY
AFDHMQIEEL ARKGGYVTYA GKQCTEYAVA NSAARVCAAV LHNEHAVLSA STLMTGQYGE
EGIFTSLPCV IGAEGVEEVY TLDLSERELE GFHKSCQHIR DNIAQLDWWD EAAWNAK
//
