ID A0A060NI11_9BURK Unreviewed; 329 AA.
AC A0A060NI11;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lactate dehydrogenase and related dehydrogenase {ECO:0000313|EMBL:BAO80842.1};
GN ORFNames=SRAA_0988 {ECO:0000313|EMBL:BAO80842.1};
OS Serpentinimonas raichei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO80842.1, ECO:0000313|Proteomes:UP000067461};
RN [1] {ECO:0000313|EMBL:BAO80842.1, ECO:0000313|Proteomes:UP000067461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:BAO80842.1,
RC ECO:0000313|Proteomes:UP000067461};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AP014568; BAO80842.1; -; Genomic_DNA.
DR RefSeq; WP_045531281.1; NZ_AP014568.1.
DR AlphaFoldDB; A0A060NI11; -.
DR STRING; 1458425.SRAA_0988; -.
DR KEGG; cbaa:SRAA_0988; -.
DR HOGENOM; CLU_019796_1_2_4; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000067461; Chromosome.
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 CDD; cd05301; GDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000067461}.
FT DOMAIN 8..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 35367 MW; E82749F68EACA426 CRC64;
MNALRPGVLI TRRLFPEVLQ RLGEHFELRD NPQDAVWSPA ELIERLQGQW GVLATQGDRI
DASVLAACPQ LRVVANMAVG YNNLDLGALT RHGVQASNTP DVLTESTADF GLALLLATAR
RITEGERYLR AGRWNKWAAD MLLGAEVHHS TLGILGMGRI GQAIARRAAH GFSMQVIYHN
RSPLDAATER ACAARCVSKA ELLRQADHLL LVLPYTPANH HAIGAAELAQ MKPSATLVNL
ARGGIVDELA LAQALQSGQL AAAGLDVFEG EPQVRPELLA LSNVVLTPHI ASATRGTRLG
MALLAADNLV ACHQRGQLLT PINAPLPRK
//
