ID V2U5W0_9GAMM Unreviewed; 322 AA.
AC V2U5W0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Gluconate 2-dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=P253_00515 {ECO:0000313|EMBL:ESK49663.1};
OS Acinetobacter indicus CIP 110367.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341679 {ECO:0000313|EMBL:ESK49663.1, ECO:0000313|Proteomes:UP000018415};
RN [1] {ECO:0000313|EMBL:ESK49663.1, ECO:0000313|Proteomes:UP000018415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110367 {ECO:0000313|EMBL:ESK49663.1,
RC ECO:0000313|Proteomes:UP000018415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter indicus CIP 110367.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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:ESK49663.1}.
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DR EMBL; AYET01000001; ESK49663.1; -; Genomic_DNA.
DR RefSeq; WP_016658352.1; NZ_KI530745.1.
DR AlphaFoldDB; V2U5W0; -.
DR PATRIC; fig|1341679.3.peg.504; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000018415; Unassembled WGS sequence.
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000018415}.
FT DOMAIN 6..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35728 MW; 895CB93FA061F2C0 CRC64;
MKQKVIAFSQ VDQYVLSQLK QQYDLVEISP KLGDVNEQIR THVQDADGMI GAGRLLNASN
LTGARRLKVV SSISVGYDNY DVDYLTEQKI YLCHTPHVLT ETTADLAFSL LMGASRQLAY
LDRWTKQGEW KRTVGPAQFG QDIHGKTLGV IGLGNIGAAI ARRGRYGFNM NILYHNRREN
LAQAQPLNAQ YRSLDELLQQ SDFVVVAVDL NADSTALIGA REFELMQKHA VFVNIARGSV
VNEQALIDAL KQQKIFAAGL DVYEKEPLQS SELFNLDNVV TLPHIGSATA ETRKKMAWLA
YKNLVDVLEG RQPGYAVNGG FA
//
