ID U1GHG4_9ACTN Unreviewed; 321 AA.
AC U1GHG4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:ERF57570.1};
GN ORFNames=H641_02788 {ECO:0000313|EMBL:ERF57570.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF57570.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF57570.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF57570.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:ERF57570.1}.
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DR EMBL; AOSS01000084; ERF57570.1; -; Genomic_DNA.
DR RefSeq; WP_021103576.1; NZ_AOSS01000084.1.
DR AlphaFoldDB; U1GHG4; -.
DR PATRIC; fig|1160719.4.peg.533; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000016307; 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; IPR029753; D-isomer_DH_CS.
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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000016307}.
FT DOMAIN 30..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 34307 MW; D88D273889825D18 CRC64;
MKRIVVTAPQ LTDIVARELD GCEIIGGGHA MTREELAEQI VEADALLSSL SDPLDADILA
RATKLEVIGQ CAAGFNNIDV DAARDRGIVV TTTPGVLHET TADLAFGLML MVTRRLGEAE
RYVRAKQPWH YDHTFMLGMG LQGATLGIIG LGQIGEAMAR RAAAFGMDVV YTARHDKDAS
AIDATNPSTA PTRRVELDEL LRTSDVVSVH CPLTEQTRHI IDAGALAAMK STAYLVNTAR
GACVDEKALV TALRNGEIAG AGLDVYENEP DIEPELYDMD NVVLLPHIGS AARRTREKMT
ELAARNIAAV LGGKDALTPV G
//
